Innovative Food Science and Emerging Technologies 62 (2020) 102368

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Innovative Food Science and Emerging Technologies

journal homepage: www.elsevier.com/locate/ifset

Cooking evaluation of crayfish (Procambarus clarkia) subjected to microwave T

and conduction heating: A visualized strategy to understand the heat-
induced quality changes of food
Hailong Fana,c, Daming Fana,b,c, , Jianlian Huangb,d, Jianxin Zhaoa,c, Bowen Yana,c,
⁎

Shenyan Maa,c, Wenguo Zhoub,d, Hao Zhanga,c

a
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China
b
Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China
c
School of Food Science and Technology, Jiangnan University, Wuxi 214122, China
d
Fujian Anjoyfood Share Co. Ltd., Xiamen 361022, China

ARTICLE INFO ABSTRACT

Keywords: The evaluation of food cooking process is an important way to understand the heat-induced quality changes and
Microwave optimize the heating process. To understand the quality changes in crayfish tail heated by microwave (MW) and
Crayfish boiling water (BW), the protein denaturation, cooking uniformity and overheating degree of tails were visually
Cooking evaluation evaluated based on the theories of reaction kinetics and maturity value in this work. Protein denaturation
Boiling
analysis showed that heat-induced protein denaturation in crayfish tails heated by MW and BW followed first-
Reaction kinetics
order reaction kinetics and had similar one-dimensional denaturation patterns and temperatures, but their
Maturity value
distributions were non-uniform and with reverse trends. Moreover, strong correlations between protein dena-
turation degree and heat-induced qualities changes were observed in crayfish tail during heating. The cooking
uniformity and overheating degree of crayfish tail heated by MW and BW were evaluated by the maturity value
(Mv) and overheating value (Ov), respectively. Evaluations showed that the profiles of Mv and Ov in the crayfish
tail were non-uniform and with reverse trends, and there was lower ΔMv and Ov for crayfish tail heated by MW
than by BW, but higher Ov occurred in the centre, which corresponded to the texture of crayfish tails heated by
MW was more susceptible than by BW when proteins had completely denatured.
Industrial relevance: The general patterns of cooking process in crayfish tail during microwave heating and
boiling have been visually evaluated and compared based on the theories of reaction kinetics and maturity value,
which enriched the knowledge for the application of microwave in the industrial thermal processing of crayfish
and reaction kinetics in the analysis of cooking (especially microwave heating). Furthermore, the theory of
maturity value was introduced into the evaluation of the cooking uniformity and overcooked degree in crayfish
tail during the heating, which provided a new strategy for the cooking evaluation of food.

1. Introduction
Crayfish (Procambarus clarkia), a kind of freshwater shellfish with
delicious meat and rich nutrition, has become one of the fastest growing
aquatic products in China (Shao et al., 2018). In recent years, the
processed products of off-season crayfish have increased rapidly and the
main products include deep-frozen crayfish tails and whole or seasoned
crayfish (Gillespie, Nyaupane, & Boucher, 2012). Most products usually
require heat treatment to cook the meat or inactivate endogenous en-
zymes and pathogenic microorganisms during processing (Ling, Tang,
Kong, Mitcham, & Wang, 2014). Traditional heat treatments of crayfish
mainly include boiling, frying, baking, etc., and boiling is one of the
most widely used heat treatments (Moody, 1989). However, the pro-
blems of low efficiency, high nutrient loss and wastewater pollution in
traditional processing methods (boiling or frying) of crayfish are be-
coming more and more prominent with the rapid increase of demand
for crayfish processing in China.
Microwave (MW) heating, which is a type of dielectric heating
without requiring any heat-transfer medium, has been widely used in
food processing (Chandrasekaran, Ramanathan, & Basak, 2013; Eng,
Emmanuel, Eng, & Omosun, 2014). Compared with the traditional
boiling, MW heating has the advantages of high efficiency, eco-

⁎
Corresponding author at: State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
E-mail address: fandm@jiangnan.edu.cn (D. Fan).

https://doi.org/10.1016/j.ifset.2020.102368
Received 13 February 2020; Received in revised form 20 April 2020; Accepted 21 April 2020
Available online 30 April 2020
1466-8564/ © 2020 Elsevier Ltd. All rights reserved.
H. Fan, et al.
friendliness and more nutrients were retained (Jouquand et al., 2015).
Therefore, the application of MW in the thermal processing of crayfish
will reduce the requirement for water, which enables a greater reten-
tion of nutrients in crayfish meat and less costs or wastewater dis-
charge. However, the cooking responses and quality changes of crayfish
heated by MW and boiling water (BW) are different and unrevealed due
to the differences in the heating principles and little work have been
done. The lack of knowledge for the cooking of crayfish has limited the
application of microwave in the heating processing of crayfish. More-
over, the evaluation of food cooking process is an important way to
understand the heat-induced quality changes and optimize the heating
process.
Protein is the major organic component of crayfish meat and gives
the meat high nutrition and delicious taste (Romero, Cordobés,
Guerrero, & Puppo, 2011). Protein denaturation is the most important
change during the cooking of crayfish, which affects the hydro-
phobicity, aggregation and gel properties of proteins, and thus affects
the qualities of food such as color and texture (Ishiwatari, Fukuoka, &
Sakai, 2013; Tornberg, 2005). However, the denaturation of proteins in
crayfish is a complex dynamic process in heat processing. It is related to
the heating histories or temperature responses of food. Usually, there
are different uniformities in temperature distribution and degree of
protein denaturation during the heating process of food due to the
different heating rates in different parts of the food (Ishiwatari et al.,
2013). However, excessive denaturation and incomplete denaturation
of proteins have great impacts on the food quality and safety, especially
in MW heating (Vadivambal & Jayas, 2010). Therefore, the quickly
control and visually predict this complex process is an important way to
improve the heat processing and quality of crayfish.
Raman spectra, circular dichroism, infrared spectroscopy, SDS-
PAGE and differential scanning calorimetry (DSC) are commonly used
in the study of protein denaturation, but DSC analysis is considered to
be the most effective way to explore the dynamic denaturation of
protein in a mixed protein system (Herrera, Pastoriza, & Sampedro,
2001). Some previous researches have successfully applied the reaction
kinetics to the protein denaturation analysis of seafood (shrimp or
prawn or fish) or meat (pork or beef) during conduction heating based
on DSC analysis (Ishiwatari et al., 2013; Li, Llave, Mao, Fukuoka, &
Sakai, 2018; Liu, Yu, Fukuoka, & Sakai, 2014; Llave, Yu, Fukuoka, &
Sakai, 2014; Mao et al., 2016; Wang et al., 2018). However, these
studies were limited to conduction heating, and there are few reports
about microwave heating or the comparison between conduction and
microwave heating. Furthermore, although protein denaturation degree
significantly affects the muscle quality, it cannot completely describe
the relative cooking degree of food and it is difficult to show the phe-
nomenon of overheating. Deng (2013) proposed a new dynamic func-
tion (maturity value or M value) for the cooking based on cook value (C
value) proposed by Mansfield (1962) for the aseptic process of low acid
food, and was successfully used to describe the equivalent changes of
cooking quality factors in the cooking of Chinese food.
In this work, the theories of reaction kinetics and maturity value,
which based on DSC analysis, were used to explore and visually eval-
uate the cooking process (including protein denaturation, cooking
uniformity and overheating degree) of crayfish heated by MW and BW,
and the corresponding heat-induced quality changes (including cooking
loss, moisture content, color and texture) of crayfish tail during heating
to provide theoretical basis for the cooking evaluation and optimization
of the heat processing of crayfish and even all the high-protein food.
2. Materials and methods
2.1. Samples of crayfish
Fresh crayfish were purchased from Xuelang Fishery Market (Wuxi,
Jiangsu, China) in the harvest season (June to September) and im-
mediately transported to the laboratory at 0–4 °C to maintain vitality.
2
Innovative Food Science and Emerging Technologies 62 (2020) 102368
Crayfish with a similar body weight (30 ± 3 g), size (9 ± 1 cm) and
apparent color (red shell) were selected as the experimental samples
and analyzed within 48 h.
2.2. Thermal treatments
The crayfish were immersed in an ice water bath for 60 min to in-
duce unconsciousness and divided into 24 groups. Ten groups, which
without packaging and each was placed in a cylindrical glass bowl,
were respectively heated for 0, 30, 60, 90, 120, 150, 180, 210, 240 and
270 s at 3 W/g (power: 250 W, sample load: 83 ± 3 g) in a microwave
oven (Model NN-7251WBGTG, Panasonic, Osaka, Japan) equipped with
a rotating turntable (rotation rate, 5 r/min); the rest of groups without
packaging were respectively heated for 0, 10, 20, 30, 40, 50, 60, 90,
120, 150, 180, 210, 240 and 270 s by BW (99 ± 1 °C). After heating,
the crayfish were immersed in ice water immediately and cooled to
room temperature for analysis. The above treatments of each group
were repeated to ensure sufficient samples (6/group) for analysis and at
least 144 crayfish were needed in one study lot.
2.3. DSC measurement
DSC was used to analyze the thermal denaturation temperature and
enthalpy of the protein. In order to improve the representativeness of
sampling, the central meat (about few mm3 in volume) of the second
tail segments of crayfish treated as Section 2.2 mentioned were col-
lected and homogenized (at temperature < 4 °C) into mince by a
precooled grinder (A11 basic, IKA Inc., Guangzhou, China), respec-
tively. Then approximately 15 mg each were chosen randomly from the
mince samples and hermetically sealed in 40 μl aluminium sample pans,
and an empty aluminium pan was used as a reference for DSC mea-
surement in the instrument (DSC3, Mettler Toledo, Switzerland). Both
samples and reference were heated over the range from 25 °C to 100 °C
at different heating rates (5, 7.5, 10, 12.5, 15, 17.5 and 20 °C/min) for
the unheated (raw) group and at 10 °C/min for heated groups. The
denaturation peak temperatures [Tmax (K)] of proteins in the unheated
meat sample measured at different heating rates and the protein de-
naturation enthalpy [ΔHt (kJ/g)] of samples heated for different time
were recorded. At least three parallel samples were measured to ensure
the reliability of the results.
2.4. Measurement of temperature profiles in crayfish tails
The measurable isothermal map, which is more accurate than nu-
merical simulation and more immediate than infrared thermal imaging,
was used to measure the temperature profiles of crayfish tail in this
study. Five optical fiber thermometers (FOT-L-SD-C1-F1-M2-R1-ST,
Fiso, Canada) and an infrared thermal imager (IRI4010, Northants
N49BG, Irisys, UK) were respectively used to monitor the internal
temperature and determine the surface temperature of the second tail
segment [the thickest part and can best describe the quality of shrimp
tail (Nunak & Schleining, 2011)] of crayfish heated for 270 s by MW at
3 W/g or BW. The positions (A, B, C, D and O) of optical fiber ther-
mometers as shown in Fig. 1 and temperatures of five points were re-
corded by a computer. The treatment of each group was repeated 3
times to obtain the average temperature of each point. According to the
time-temperature curve of five points and surface in the tail, the tem-
perature profiles of cross section in the second tail segment of crayfish
heated by MW or BW were drawn by Surfer 15.0 (Golden Software Inc.,
USA) which has powerful functions of interpolation and drawing iso-
gram (Yang et al., 2019).
2.5. Measurement of cooking loss of crayfish and moisture content of
crayfish tail
The weight of the crayfish were recorded before and after heating,
H. Fan, et al.
Fig. 1. Diagram of temperature monitoring points (A, B, C, D, O) of cross section in the second tail segment of crayfish.
and cooking loss [CL(%)] of the whole crayfish was calculated ac-
cording to following equation (Eq. (1)) for each group (Vittadini,
Rinaldi, Chiavaro, Barbanti, & Massini, 2005):
CL = (Mi Mj)/Mi × 100%,
where Mi (g) and Mj (g) represent the weights before and after heating,
respectively. The results were reported as the average of 6 repetitions.
About 5 ± 0.5 g homogenized tail meat of each group were
weighed and dehydrated to a constant weight in an oven (FD115,
Binder GmbH, Tuttingen, Germany) at 105 °C. All of the measurements
were performed in triplicate, and the moisture content [MC (%)] was
calculated by Eq. (2) (Li, Li, & Zhang, 2018; Tanaka, Mallikarjunan, &
Hung, 1999):
MC = (Wi W)/W
j i × 100%,
where Wi (g) and Wj (g) represent the weights of the tail sample before
and after dehydration, respectively.
2.6. Measurement of crayfish tail color
The tails of crayfish heated as described in Section 2.2 were peeled
and then cut into 10 ± 0.5-mm pieces vertically along the direction of
the second tail segment. The cross-section RGB images of the tails were
obtained using a digital camera (Nikon D7200, Nikon Corporation,
Japan) in an image acquisition system equipped with a D65 standard
light source. The cross-section L⁎, a⁎ and b⁎ values of the tail pieces
were measured using a colorimeter (Ultra Scan Pro 1166, Hunterlab
Inc., USA). Here, L⁎ represents lightness, a⁎ represents redness (+) or
greenness (−) and b⁎ represents yellowness (+) or blueness (−). The
total color difference (ΔE) of the L⁎, a⁎ and b⁎ was calculated by Eq. (3).
Innovative Food Science and Emerging Technologies 62 (2020) 102368
L⁎0, a⁎0 and b⁎0 represent the cross-section L⁎, a⁎ and b⁎ of the unheated
crayfish tail segment, respectively.
E= (L L 0 )2 + (a a 0)2 + (b b0 ) 2 (3)
(1)
2.7. Measurement of crayfish tail texture
The measurement of crayfish tail texture (including surface hard-
ness, springiness, internal hardness and compactness) referred to our
previous invention patent (CN 109270231A). The peeled whole tails
(6/group) from crayfish heated as described in Section 2.2 were placed
on the loading platform of a TA-XT2 texture analyzer (Stable Micro
Systems, Ltd., Surrey, UK). A P/5 cylindrical probe was used to measure
(2)
the surface hardness and springiness of the tails (as show in Fig. 2a).
The test parameters were as follows: pre-test speed, 1.0 mm/s; test
speed, 1.0 mm/s; return speed, 1.0 mm/s; target mode, distance and
time; compression distance, 3.0 mm; hold time, 30 s and trigger force,
5 g. The force (F1) given to the probe when the tail was compressed by
3 mm was defined as surface hardness (N), and the ratio of the force
(F2) maintained compression for 30 s to surface hardness was defined
as springiness (F2/F1). Next, the P/5 cylindrical probe was replaced
with a P/2 cylindrical probe, which was used to measure the internal
hardness and compactness of the tails (as show in Fig. 2b). The test
parameters were as follows: pre-test speed, 1.0 mm/s; test speed,
1.0 mm/s; return speed, 1.0 mm/s; target mode, distance; depth of
puncture, 90% of the crayfish tail height and trigger force, 5 g. The
maximum positive peak force during the puncture was defined as in-
ternal hardness (N) and absolute value of maximum negative peak force
was defined as compactness (N). Finally the surface hardness,
3
H. Fan, et al. Innovative Food Science and Emerging Technologies 62 (2020) 102368

Fig. 2. The measurement of surface hardness and springiness of crayfish tails and its texture plot (a), and the measurement of internal hardness and compactness of
crayfish tails and its texture plot (b).

springiness, internal hardness and compactness of the crayfish tails follow the first-order chemical reaction kinetics equation [Eq. (4)] as
were determined. reported in prawn or pork during conduction heating (Kajitani,
Fukuoka, & Sakai, 2011; Mao et al., 2016). Eq. (4) was dealt with di-
2.8. Statistical analysis mensionless to obtain Eq. (5), and it was simplified to Eq. (6). The k
(/min) is the reaction rate constant and changed with temperature,
The tests were repeated at least three times, and the data obtained which can be expressed by Arrhenius equation, as show in Eq. (7).
in the tests were expressed as the means ± standard deviations.
dC
Statistical analyses of variance (ANOVAs) were performed by Microsoft = kC
dt (4)
Excel 2010. Paired-t-tests to test differences between the experimental
and predicted non-denaturation ratio of protein were performed with d Ct dX Ct
IBM SPSS Statistics 19.0 (SPSS Inc., Chicago, IL, USA). Multiple com- = = k(T) = k(T)X
dt C 0 dt C0 (5)
parisons of mean values were conducted using Duncan's multiple range
test. lnX = k(T)t (0 X 1) (6)

3. Theoretical calculation Ea
k(T) = Ze RT (7)

3.1. Calculation of kinetic parameters of protein denaturation
According to the hypothesis of the two-state model, Villota and
Hawkes (2006) supposed that the thermal denaturation rate of protein
was proportional to the concentration of non-denatured protein
(Robinson, Urquidi, Singh, & Cho, 2001), and thus the protein dena-
turation rate in crayfish tail heated by MW and BW were assumed to
where C (mol/g) is the concentration of non-denatured protein; t (min)
is the reaction time; C0 (mol/g) is the initial concentration of protein. Ct
(mol/g) is the concentration of non-denatured protein at t min, and X
represents Ct/C0 as the ratio of non-denatured protein; Z (/min) is the
pre-exponential factor in Arrhenius equation, Ea (kJ/mol) is the protein
denaturation activation energy, R [J/(mol·K)] is the gas constant, and T
(K) is the temperature.

4
H. Fan, et al. Innovative Food Science and Emerging Technologies 62 (2020) 102368

When the heating at a constant rate in DSC measurement, there is a t Ti Tref

relationship between heating temperature and heating time, as shown Mv (t) = 10 Zm dt

(16)
in Eq. (8). Based on Eqs. (5), (7) and (8), we obtained Eq. (9).
0

(t j ti)
dT = dt (8) D=
log(Xti) log(Xtj) (17)
dX Ea
= ZXe RT
dt (9) T(ti) T(t j)
Zm =
log(Dti) log(Dtj ) (18)
where β (°C/min) is the heating rate. Furthermore, DSC curve expressed
d(ΔHT)/dt as a function of T or t, and Eq. (10) was established when the where Ti is the cooking temperature (°C) and Tref is the reference
T reached the peak temperature of protein denaturation (Tmax). Further temperature (°C); tj and ti are the heating time (min); Xti and Xtj are the
differential treatment of Eq. (9), we obtained Eq. (11). ratios of total protein non-denaturation at ti and tj, respectively; Dti and
Dtj are the D value (min) at ti and tj, respectively; T (ti) and T (tj) are the
d2X
=0 temperature (°C) at ti and tj, respectively.
dT2 (10)
T = Tmax In this work, the non-denaturation ratio of total protein was con-
sidered as the cooking quality factor to monitor the cooking process of
d2X Z Ea Ea Ea
crayfish tail during heating. Therefore, the Mv at any point of crayfish
= e RT + Xe RT
Z dT2 RT 2 (11) tail can be calculated by Eq. (16) based on the time-temperature curve
[T(t) or Txy (t) and even Txyz (t)] of the tail during heating. In order to
Based on Eqs. (10) and (11), we obtained Eq. (12)
describe the cooking uniformity of crayfish tail, we introduced ΔMv (s)
ZR Ea (as shown in Eq. (19)) which referenced to the concept of variation of
ln = ln
T 2max Ea RTmax (12) color (ΔE). Therefore, the higher ΔMv is, the worse cooking uniformity
is. Furthermore, we defined that the crayfish tail was cooked when the
where Tmax (K) is the peak temperature corresponding to the en- proteins denaturation of crayfish tail were concluded (Xtotal = 0.001)
dothermic peak of protein denaturation. (Kajitani et al., 2011), and the subsequent heating was overheating.
A plot (Ozawa curve) of ln ( ) vs. 1 / T
T 2max
max was obtained ac- Therefore, the overheating value [Ov (s)] of crayfish can be expressed
by Eq. (20) and the average overheating value [O v (s)] of crayfish can
cording to Eq. (12) and Tmax at different heating rates (β), and its slope
and intercept were used to calculate Z and Ea (Kajitani et al., 2011). be expressed by Eq. (21).

Mv = (Mvi Mv 2
ref ) (19)
3.2. Calculation of protein denaturation degree
t Ti Tcom dena
Based on Eqs. (6) and (7), we obtained Eq. (13). The protein non- Ov (t) = 10 Zm dt
denaturation ratio [X(t)] of any point in the cross section of the second 0 (20)
segment of crayfish tail was calculated according to Eq. (13) and the
Oxy (t) = Average(Ov1 , Ov2 , Ov3……Ovi) (21)
time-temperature curve [T(t)] of tail. The total protein non-denatura-
tion ratio (XTotal), as shown Eq. (14), was used to represent the total where Mvi (s) is the maturity value at any point, and Mv-ref (s) is ma-
denaturation process of the major proteins (myosin, sarcoplasmic pro- turity value of the reference point; Ti is the temperature (°C) at any
tein and connective tissue proteins, actin) in crayfish tail (Mochizuki, point of crayfish tail and Tcom-dena is the temperature (°C) when protein
Mizuno, Ogawa, & Iso, 1995). completely denatured.
Ea
X(t) = e ZeRT(t) t
(13) 4. Results and discussion

XTotal (t) = P1XMyosin + P2 XSarco con + P3 XActin
where XMyosin, XSarco-con and XActin are the denaturation ratios of
myosin, sarcoplasmic protein and connective tissue proteins, and actin,
respectively. P1, P2, P3 are the ratios of thermal denaturation enthalpy
for the three kinds of proteins at native, respectively.
X xy(t) was used to represent the average protein non-denaturation
ratio in the cross section of the second segment of crayfish tail (Eq.
(15)).
Xxy (t) = Average(X1, X2 , X3……, Xi)
where Xi is the protein non-denaturation ratio of any point in the plane.
3.3. Calculation of maturity value of the crayfish tail
(14) 4.1. Kinetic parameters of thermal denaturation of protein
A typical DSC curve with three obvious endothermic peaks for the
DSC measurement of the unheated meat sample at a heating rate of
10 °C/min was showed in Fig. 3a. According to the Tmax of the three
peaks (50.00, 68.00 and 85.67 °C, respectively) and previous researches
(Bertram, Wu, van den Berg, & Andersen, 2006; Schubring, 2009; Shao
et al., 2018; Wang et al., 2018), they corresponded to the myosin
(50 °C), sarcoplasmic protein and connective tissue proteins (mainly
(15) collagen) (65 °C) and actin (80 °C), respectively. Therefore, protein
denaturation was an endothermic reaction, and the denaturation tem-
peratures varied with different proteins (Bertram et al., 2006). Fur-
thermore, each Tmax of protein shifted to a higher temperature with the
increasing of heating rate (β). As shown in Fig. 3b, the ln ( ) for
T 2max

Deng (2013) applied the definition of cooking value (C value) to the
cooking process of food, and proposed a new concept of maturity value
(Mv) (Eq. (16)). It was the equivalent heating time for the measuring
point and reference point when their cooking quality factor achieved
the same cooking degree in their respective heating histories, which
depended on the heating history (Deng, 2013). Where Zm represents the
temperature (°C) required for the D value [the time required for the
cooking quality factor to change one logarithmic unit, as shown in Eq.
(17)] to change one logarithmic unit, as shown in Eq. (18).
the three major proteins of the crayfish tail varied linearly with 1
Tmax
(defined as Ozawa curve). The Ea, Z and k of the major proteins in the
crayfish tail were calculated by the slope and intercept of the Ozawa
curve, and the calculated values were shown in Table 1. The results
were similar to those reported in previous literatures (Ishiwatari et al.,
2013; Kajitani et al., 2011). Actin had the highest denaturation acti-
vation energy and myosin had the lowest. In other words, the thermal
stability of the three major proteins was actin > sarcoplasmic protein
and connective tissue proteins > myosin.

5
H. Fan, et al.
Fig. 3. DSC curve (at β = 10 °C/min) (a) and Ozawa curve (b) of the three major proteins in crayfish tails. Sarco-con represents the sarcoplasmic protein and
connective tissue proteins.
Table 1
Kinetic parameters (Ea, Z and Zm) of thermal denaturation of protein and the
ratio of thermal denaturation enthalpy for three kinds of major proteins.
Ea (kJ/mol) Z (/min) k (/min) P Zm (°C)
Myosin 257.53 7.55 × 1041 Ea 0.6 7.15
Sarco-con proteins 282.57 3.16 × 1043
Ze RT
0.25
Actin 340.22 6.98 × 1049 0.15
Sarco-con proteins is the abbreviation of sarcoplasmic protein and connective
tissue proteins. Ea is protein denaturation activation energy and Z is pre-ex-
ponential factor in Arrhenius equation. The k is reaction rate constant and P is
the ratio of thermal denaturation enthalpy for the major proteins. Zm represents
the temperature required for the D value of Xtotal to change one logarithmic
unit.
4.2. Temperature profiles in crayfish tail during heating
Microwave, as a kind of dielectric heating, can simultaneously heat
both the inside and the outside of the food, which is different from
conduction heating (Acevedo, Usón, & Uche, 2014; Chandrasekaran
et al., 2013). However, the phenomenon of uneven heating exists in
both microwave and conduction heating, which is attributed to the
complex shape and heat conduction of the heated object. As shown in
Fig. 4a, there are different heating histories for the different points of
cross section in the second tail segment of crayfish heated by MW and
BW. Influenced by the accumulation of energy (e.g., focusing effect or
microwaves resonance) in the centre of the cylindrical crayfish tail
(Hossan, Byun, & Dutta, 2010), the cross-section temperature profiles in
the second tail segment of crayfish heated by MW showed a gradient
distribution decreasing from the inside to the surface (Fig. 4b). How-
ever, the cross-section temperature profiles in the second tail segment
of crayfish heated by BW showed a reverse trend of MW heating
(Fig. 4b), which was attributed to their different temperature between
the inside and outside of the tail. Furthermore, the non-uniformity of
the temperature profiles for the boiled crayfish tail were obvious in the
first 60 s, but it tended to be uniform in the last 210 s with increasing of
heating time and decreasing of heating rate. The uniformity of the
temperature profile for crayfish tail heated by MW in the early stage
(≤90 s) and last stage (210–270 s) was higher than that in the middle
stage (90–210 s), which might be attributed to the temperature of hot
spots increased rapidly with increasing time until it was maintained due
to the water evaporation and then overall temperature tended to bal-
ance driven by heat conduction. This indicated that crayfish heated by
MW were more likely to be unevenly heated in the middle stages, while
6
Innovative Food Science and Emerging Technologies 62 (2020) 102368
BW was more likely in the early stage.
4.3. Denaturation kinetics of protein in crayfish tail during heating
4.3.1. One-dimensional protein denaturation
When the temperature gradually increases to the denaturation
temperature, the protein structure will change irreversibly. This process
is related not only to temperature but also to heating rate (Lefevre,
Fauconneau, Thompson, & Gill, 2007). As shown in Fig. 5a and b, three
kinds of major proteins at point O of the crayfish tail heated by MW and
BW gradually denatured with increasing temperature in the same trend,
and the sequence of denaturation and denaturation rate were consistent
with their thermal stability. However, there was a higher maximum
protein denaturation rate at point O of the tails heated by MW than BW.
This result might be attributed to the instantaneous heating rate of
point O for the heating of MW was higher than that of BW at a certain
moment (Fig. 5c). In addition, the temperatures (48.00, 63.30 and
80.15 °C) corresponding to the maximum denaturation rate of the three
kinds of proteins were similar to their denaturation temperatures
measured by DSC at the heating rate of 10 °C/min. Thus, we considered
the kinetic parameters determined in Section 4.1 were appropriate. The
ratios of thermal denaturation enthalpy (P1, P2 and P3) for the three
kinds of proteins were calculated and shown in Table 1. The order of
ratios of thermal denaturation enthalpy (P1 > P2 > P3) was con-
sistent with the fact that the content of myosin (4.73%) > sarco-
plasmic protein (3.85%) and connective tissue proteins
(0.13%) > actin (3.15%)in the proteins of shrimp tail (Niamnuy,
Devahastin, & Soponronnarit, 2008; Sriket, Benjakul, Visessanguan, &
Kijroongrojana, 2007). When the denaturation degree of protein was
expressed by the total non-denaturation ratio of protein (XTotal), the
protein denaturation at point O for the boiled tail was prior to that of
MW heating and the maximum denaturation rate was lower than that of
MW heating, but their complete denaturation temperature (83.15 and
82.9 °C, respectively) of protein was approached (Fig. 5d). This was
because the temperature at point O for the boiled tail was higher than
that of MW heating at the same time, but its heating rate was lower
than that of MW heating during the denaturation period of protein
(Fig. 5c). Therefore, compared with boiling, the protein denaturation at
point O of the tail heated by MW at 3 W/g took more time but was more
rapid. And the temperature of protein denaturation was not affected by
heating methods.
4.3.2. Experimental verification of one-dimensional protein denaturation
The ratio of the thermal denaturation enthalpy of protein (ΔHt) at t
H. Fan, et al.
Fig. 4. Time-temperature curves of different temperature monitoring points (including A, B, C, D, O and the surface of tail) (a) and the visual temperature profiles of
the cross section in the second tail segment of crayfish during the heating (b). The different colors on the color scale indicate different temperatures.
(s) to the thermal denaturation enthalpy of natural protein (ΔH0) was
proportional to the non-denaturation ratio of protein (Cao, Tian, Wang,
Liu, & Wang, 2014). Therefore, ΔHt/ΔH0 obtained by DSC analysis can
be used to represent the true non-denaturation degree of protein during
the heating. As shown in Fig. 6a and b, the trends of ΔHt/ΔH0 at point O
changed with the heating time of MW and BW, which were consistent
with the theoretical calculation results in Section 4.3.1 (R2 values were
0.88 and 0.95, respectively) and there was no significant difference
(P > 0.05) between the experimental and calculated ratio of total non-
denaturation protein. Although the calculated results of protein non-
denaturation ratio lagged behind the experimental results, which was a
normal performance for the sampling of experiment could not be ac-
curate to the point. Therefore, the protein denaturation at point O of
crayfish tail heated by MW and BW can be accurately predicted by the
first-order reaction kinetics model.
4.3.3. Two-dimensional protein denaturation
As described in the one-dimensional protein denaturation, the pro-
tein denaturation at point O of the crayfish tail depended on its heating
histories. Therefore, there was asynchronous protein denaturation at
different points with different heating histories in the crayfish tail. As
shown in Fig. 7a, the cross-section protein denaturation profiles (two-
dimensional protein denaturation profiles) in the second tail segment of
crayfish heated by MW showed a gradient distribution decreasing from
the inside to surface until the protein had completely denatured, while
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Innovative Food Science and Emerging Technologies 62 (2020) 102368
that of boiled crayfish was reverse (Fig. 7b). These results corresponded
to their temperature profiles. Moreover, there was modest protein de-
naturation until 60 s and the major denatured protein was myosin in
the internal area with higher temperature for the crayfish heated by
MW, which was attributed to its slow initial heating rate and the lowest
denaturation temperature of myosin. When the temperature rose to the
higher denaturation temperature of protein (50–80 °C), the sarco-
plasmic protein, connective tissue protein and actin began to denature,
and denaturation degree of total protein in the second cross section of
the crayfish tail began to increase rapidly. Until 150 s, the denaturation
profiles of the total protein in the second tail segment of crayfish heated
by MW tended to be uniform since most of protein had completely
denatured except for a small amount of actin (Fig. 7a and c). However,
the uniformity of the protein denaturation profile for the cross section
in the second tail segment of boiled crayfish was poor in the first 60 s
(i.e., a big variance for average protein non-denaturation ratio of cross
section), and then tended to be uniform in the last 210 s (Fig. 7b and d).
This was attributed to the large temperature difference between the
surface and the centre of the crayfish tail that was in direct contact with
BW in the early stage gradually became uniform with increasing
heating time.
4.4. Mature kinetics in the crayfish tail during heating
Protein denaturation is the major change in crayfish tail during
H. Fan, et al. Innovative Food Science and Emerging Technologies 62 (2020) 102368

Fig. 5. The non-denaturation ratios of three major proteins at point O during MW heating (a) and boiling (b) as well as the heating rates (c) and total protein non-
denaturation ratio (d) at point O. The temperatures indicated by arrow in d were the complete denaturation temperatures of BW and MW, respectively.

Fig. 6. Comparison of the measured and calculated total non-denaturation ratio of protein at point O for MW heating (a) and boiling (b). R2 is the Pearson correlation
coefficient and P is the level of the difference test, P > 0.05 indicated there was no significant difference.

8
H. Fan, et al. Innovative Food Science and Emerging Technologies 62 (2020) 102368

Fig. 7. The visual protein denaturation profiles of the cross section in the second tail segment of crayfish heated by MW (a) and BW (b), and the average protein non-
denaturation ratios of the cross section in the second tail segment of crayfish heated by MW (c) and BW (d). The different colors on the color scale indicate different
protein non-denaturation ratios. X Myosin is the average protein non-denaturation ratio of myosin; X Sarco-con is the average protein non-denaturation ratio of sarco-
plasmic protein and connective tissue proteins; X Actin is the average protein non-denaturation ratio of actin.

9
H. Fan, et al.
Fig. 8. The Mv profiles (a) and ΔMv (b) of the cross section in the second tail segment of crayfish heated by MW and BW. The different colors on the color scale
indicate different Mv; the Mv is maturity value and ΔMv is the variation of Mv at different points.
heating, but the degree of protein denaturation cannot represent the
relative cooking degree of food when the protein has completely de-
natured, especially when subjected to overheating. The maturity value
(Mv) has been used to describe the equivalent treatments to achieve the
same cooking degree of cooking quality factor of food. It is a process
function which can evaluate the accumulative changes of cooking
quality factor over time. When the ratio of total protein denaturation
was used as a cooking quality factor, the Zm was calculated by Eqs. (17)
and (18), and shown in Table 1, which was in the range of 4–10 °C
reported by Rao, Rizvi, Datta, and Ahmed (2014). In this work, the
cooking uniformity was evaluated by Mv or ΔMv. when the point O was
considered as the reference point. As shown in Fig. 8a, the Mv profiles of
the cross section in the second tail segment of crayfish heated by MW
were relatively uniform in the first 90 s and then an area (near the
centre or abdomen of tail) with higher Mv was appeared in the last
180 s, while that of boiled crayfish tails showed a trend that Mv of
surface was much higher than centre after heating for 20 s and then
maintained. These trends were digitized by the ΔMv in the Fig. 8b. In
other words, the cooking degree in the area where near the centre or
abdomen of tail heated by MW was higher than the surface, while the
surface was far higher than the centre for the boiled crayfish tail, which
were attributed to their temperature responses. Furthermore, the ΔMv
of boiled crayfish tail was far higher than that of crayfish heated by
MW, which indicated that the cooking uniformity of crayfish tail heated
by MW was higher than that of boiled.
When 83 °C (determined by the results described in Section 4.3.1)
10
Innovative Food Science and Emerging Technologies 62 (2020) 102368
was defined as the complete denaturation temperature of protein, the
overheating degree of crayfish tail was evaluated by the Ov. As shown
in Fig. 9b, the O̅ v of the cross section in the second tail segment of
crayfish heated by MW kept at a very low level in the first 150 s until it
rapidly increased to the maximum (16,399 s) at last 120 s, while that of
boiled crayfish continuously increase to the maximum (23,930 s) and
was always higher than MW. It indicated that there was no obvious
overheating until 180 s for the crayfish tail heated by MW at 3 W/g,
while boiled crayfish tail was always overheating and more obvious.
Furthermore, the area where near the centre or abdomen of tail was
more easily to be overheated for the crayfish tail heated by MW, while
the surface for boiled crayfish tail (as the Ov profiles shown in Fig. 9a).
4.5. Cooking loss of crayfish and change of moisture content in crayfish tail
during heating
As shown in Fig. 10, the CL of crayfish heated by MW rapidly in-
creased from 0% to 17.42% with the increasing time (especially last
150 s), while that of boiled crayfish changed slightly (fluctuated be-
tween −2.87% and 2.84%) and even most were negative value (the
water may be entrained by some parts, such as pereion). It indicated
that the crayfish were more easily to lose their mass during the heating
of MW than BW, which might attribute to the heating of BW was in an
environment with water, but MW was not. Moisture loss caused by
protein denaturation and muscle fiber contraction or evaporation have
been considered as the most important drivers of CL (Bengtsson,
H. Fan, et al.
Fig. 9. The Ov profiles (a) and Ov (b) of the cross section in the second tail segment of crayfish heated by MW and BW. The different colors on the color scale indicate
different Ov; Ov is overheating value and Ov is average overheating value.
Fig. 10. The cooking loss (CL) of crayfish and moisture content (MC) of crayfish
tail heated by MW and BW.
Jakobsson, & Sik, 2010). As shown in Fig. 10, the MC of crayfish tail
heated by MW decreased from 81.73% to 76.83%, while that of boiled
crayfish tail changed slightly around 80%, which were significant
proportional to the protein non-denaturation ratio (as shown in
Table 2) and corresponded to the increasing of CL or O v. However, there
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Innovative Food Science and Emerging Technologies 62 (2020) 102368
was no significant correlation between CL and the protein non-dena-
turation ratio or O v for boiled crayfish, which might be attributed to the
CL of boiled crayfish caused by protein denaturation from tail was ea-
sily covered by the contributions from other parts.
4.6. Change of color in crayfish tail during heating
In general, the color of muscle is easily affected by the protein de-
naturation or Maillard reaction during the thermal processing of meat
(Llave, Matsuda, Fukuoka, & Sakai, 2014; Yu, Llave, Fukuoka, & Sakai,
2014). As shown in Fig. 11a, the color of cross section in the second tail
segment of crayfish gradually changed from reddish brown to white or
light yellow during MW heating and boiling, and there was no sig-
nificant difference in the color for the completely denatured tail heated
by MW and BW. However, the color change of the cross section in the
second tail segment of crayfish heated by the MW mainly extended
from the centre to the surface until it tended to be uniform at ap-
proximately 150 s. In contrast, that of the boiled crayfish tails extended
from the surface to the centre and until it tended to be uniform at ap-
proximately 60 s (Fig. 11a). These results were corresponded to their
changes of temperature and total protein denaturation profiles during
MW heating and boiling, which indicated that there was a fact that
asynchronous responses of temperature and heat-induced protein de-
naturation occurred in the crayfish tail heated by MW and BW. Fur-
thermore, as shown in Fig. 11b and c, the brightness, yellowness and
redness of the cross section in the second tail segment of crayfish heated
by MW and BW changed at different degrees with increasing time. The
H. Fan, et al. Innovative Food Science and Emerging Technologies 62 (2020) 102368

Table 2
Pearson correlation coefficients among color (L⁎, a⁎, b⁎ and ΔE), texture (hardness, springiness and compactness), average non-denaturation ratios of proteins
(X Myosin, X sarco-co, X actin and X total), average overheating value (Ov), cooking loss (CL) and moisture content (MC) in crawfish tail during microwave heating and
boiling.

The upper triangle corresponds to MW heating, and the lower triangle corresponds to the boiling. *P < 0.05, **P < 0.01. Sarco-con proteins is the abbreviation of
sarcoplasmic protein and connective tissue proteins.

Fig. 11. The RGB images (a) and corresponding color value (L⁎, a⁎, b⁎) changes of the cross section in the second tail segment of crayfish heated by MW (b) and
BW (c).

12
H. Fan, et al.
L⁎, b⁎ and ΔE of crayfish tail increased obviously with increasing time
until it tended to be stable at approximately 150 s for MW heating and
at approximately 60 s for boiling, but the a⁎ fluctuated slightly. These
results were consistent with the color changes of the tail observed in the
RGB images and corresponded to the changes of protein non-dena-
turation ratio in cross section of tail (Fig. 7c and d). As shown in
Table 2, there was significant negative correlation (P < 0.05 or
P < 0.01) between the L⁎ or b⁎ or ΔE of crayfish tail and average
protein non-denaturation ratios, especially for the X Myosin, X Sarcro-con
and X Total. It indicated that the protein denaturation (especially the
high-abundance protein, such as myosin and sarcoplasmic protein)
might be the major driver of color changes in crayfish tail during
heating. That attributed to the protein denaturation or aggregation and
muscle shrinkage with increasing temperature during the heating,
which affected the reflection of light (Skipnes, Johnsen, Skara,
Sivertsvik, & Lekang, 2011). That might provide a new way to predict
the denaturation degree of protein in the crayfish tail by the tail color.
In addition, the color values of crayfish tail heated by MW were
significantly correlated to the CL and MC, while only to MC for boiled
crayfish tail. That might be attributed to there were similar trends be-
tween tail color and CL changes for the crayfish heated by MW and
opposite trend between tail color and MC changes of the crayfish heated
by MW and BW during protein denaturation. Furthermore, the b⁎ of
crayfish tail heated by MW and BW were significantly correlated to−Ov
as a result of the browning reaction during overheating (Matsuda,
Llave, Fukuoka, & Sakai, 2013).
4.7. Change of texture in crayfish tail during heating
Crawfish tail is a kind of protein-based food. Its texture is as sus-
ceptible to the changes of muscle structure caused by protein dena-
turation as other meat with high protein (García-Segovia, Andrés-Bello,
& Martínez-Monzó, 2007; Kong, Tang, Rasco, & Crapo, 2007). As shown
in Fig. 12a, the surface hardness, internal hardness, springiness and
compactness of crayfish tails heated by MW increased rapidly in the
first 90 s, and then remained stable in the 90–180 s, and finally
(180–270 s) began to decline. However, the texture of boiled crayfish
tail changed rapidly in the first 60 s and finally (60–270 s) was largely
stable at the level of crayfish tails heated for 90–180 s by the MW
(Fig. 12b). In the previous analysis of protein denaturation, we learned
that the myosin, sarcoplasmic and connective tissue proteins of crayfish
tails heated by MW and BW denatured rapidly in the first 90 s and 60 s,
Fig. 12. The changes of texture in crayfish tail heated by MW (a) and BW (b).
13
Innovative Food Science and Emerging Technologies 62 (2020) 102368
respectively, and then most proteins were denatured in 150 s and 90 s
(Fig. 7c and d), which corresponded to their changes of texture. As
shown in Table 2, there were significant negative correlations
(P < 0.05 or P < 0.01) between the non-denaturation ratios of
proteins (myosin, sarcoplasmic and connective tissue proteins, and total
protein) and the texture (surface hardness, springiness and compact-
ness) of crayfish tail. These results indicated that the denaturation and
cross-linking of proteins (especially the myosin, sarcoplasmic and
connective tissue proteins) might increase the hardness, springiness and
compactness of crayfish tail during the heating (Harris & Shorthose,
1988; Meullenet, Chang, Carpenter, & Resurreccion, 1994). Further-
more, the difference between internal hardness and surface hardness of
crayfish tail heated by MW was higher than that of boiled crayfish tail
before their hardness became stable (Fig. 12a and b), which might be
attributed to their reverse patterns of protein denaturation distribution.
It indicated that the effect of asynchronous heat-induced protein de-
naturation on the quality of crayfish tail during heating was also re-
flected in their texture.
However, continuous heating would cause excessive dehydration
and contraction of myofibrils in the crayfish tail when the protein of tail
had completely denatured, which might lead to deterioration of the
texture (Yu et al., 2014). As shown in Fig. 12a, the hardness, springiness
and compactness of crayfish tails heated by MW began to decrease in
180–270 s, which corresponded to the result that O v rapidly increased
to a larger value and MC at a low level during 180–270 s. Therefore,
overheating and it induced moisture loss might be the important factors
to cause the texture deterioration of crayfish tail heated by MW. Un-
fortunately, there were no significant correlation between texture and
O v or MC of tail heated by MW (as shown in Table 2), which might be
attributed to the texture changes of the crayfish tail included two stages
(from raw to cooked and from cooked to overcooked, respectively)
during the heating, but O v only represented the overheating stage and
the moisture loss during overheating was more easy due to evaporation
of water and contraction of myofibrils. However, it was worth noting
that the texture of the boiled crayfish tail did not change significantly
during the overheating, which might be attributed to its overcooking
mainly occurred on the surface rather than in the inside (as shown in
Fig. 9a) or the dehydration and contraction of myofibrils were weaken
in the moisture environment. When the high steam pressure was gen-
erated in the inside of tail due to overheating, the texture of crayfish tail
was more easily to be deterioration (Moore, Harrison, & Dayton, 1980;
Uzzan, Kesselman, Ramon, Kopelman, & Mizrahi, 2006).
H. Fan, et al.
5. Conclusion
A visualized method to evaluate cooking process and understand the
heat-induced quality changes of crayfish tail during the heating of MW
and BW was established. There was reverse pattern for the temperature
distribution in the second tail segment of crayfish heated by BW and
MW, which was the driver of their different cooking responses. The
denaturation patterns of three major proteins and total protein in the
crayfish tail heated by MW and BW were predicted by first-order re-
action kinetics, and the one-dimensional protein denaturation pattern
and temperature were no different in heating methods. However, there
was reverse pattern of protein denaturation distribution induced by
reverse temperature distribution in crayfish tail heated by MW and BW.
Therefore, although protein denaturation in the crayfish tail heated by
MW and BW played an important role in their qualities changes, their
quality changes were different because of the different protein dena-
turation distribution. Furthermore, the protein denaturation degree
cannot describe the cooking uniformity when protein has completely
denatured and overheating degree during heating. When the non-de-
naturation ratio of total protein was used as the cooking quality factor
of crayfish tail during the heating, the cooking uniformity and over-
heating degree of crayfish tail were successfully evaluated by Mv and
Ov, respectively. There was higher cooking uniformity and lower
average overheating degree for the crayfish tail heated by MW at 3 W/g
than by BW, but the central overheating degree of crayfish tail heated
by MW was higher than by BW, and the overheating might be con-
sidered as a more important cause for the texture deterioration of
crayfish tails heated by MW than by BW.
CRediT authorship contribution statement
Hailong Fan: Investigation, Data curation, Methodology, Writing -
original draft. Daming Fan: Conceptualization, Supervision, Project
administration, Validation, Writing - review & editing. Jianlian
Huang: Investigation, Software. Jianxin Zhao: Project administration,
Resources. Bowen Yan: Methodology. Shenyan Ma: Software.
Wenguo Zhou: Visualization. Hao Zhang: Project administration.
Declaration of competing interest
No conflict of interest exists in the submission of this manuscript,
and manuscript is approved by all authors for publication. We declare
that the work described was original research that has not been pub-
lished previously, and not under consideration for publication else-
where, in whole or in part. We declare that we do not have any com-
mercial or associative interest that represents a conflict of interest in
connection with the work submitted.
Acknowledgments
This research was financially supported by the National Natural
Science Foundation of China (31822038), the National “Thirteenth
Five-Year” Plan for Science & Technology (2019YFD0902000,
2018YFD0400600), the Open Project Program of Key Laboratory of
Refrigeration and Conditioning Aquatic Products Processing, Ministry
of Agriculture and Rural Affairs of the People's Republic of China
(KLRCAPP2018-08), the National First-class Discipline Program of Food
Science and Technology (JUFSTR20180102).
References
Acevedo, L., Usón, S., & Uche, J. (2014). Exergy transfer analysis of microwave heating
systems. Energy, 68, 349–363.
Bengtsson, N. E., Jakobsson, B., & Sik, M. D. (2010). Cooking of by oven roasting: A study
of heat and mass transfer. Journal of Food Science, 41(5), 1047–1053.
Bertram, H. C., Wu, Z., van den Berg, F., & Andersen, H. J. (2006). NMR relaxometry and
14
Innovative Food Science and Emerging Technologies 62 (2020) 102368
differential scanning calorimetry during meat cooking. Meat Science, 74(4), 684–689.
Cao, X., Tian, Y., Wang, Z., Liu, Y., & Wang, C. (2014). Protein denaturation kinetic
processes of a simple and a complex reaction mechanism analyzed by an iso-con-
versional method. Journal of Thermal Analysis and Calorimetry, 117(3), 1489–1495.
Chandrasekaran, S., Ramanathan, S., & Basak, T. (2013). Microwave food processing—A
review. Food Research International, 52(1), 243–261.
Deng, L. (2013). Kinetic functions, optimizing model and definition of “Huohou” for
Chinese cooking. Transactions of the Chinese Society of Agricultural Engineering, 29(4),
278–284.
Eng, O., Emmanuel, A., Eng, A., & Omosun, Y. (2014). Microwave application for food
processing. IOSR Journal of Electrical and Electronics Engineering (IOSR-JEEE) Volume,
9, 29–34.
García-Segovia, P., Andrés-Bello, A., & Martínez-Monzó, J. (2007). Effect of cooking
method on mechanical properties, color and structure of beef muscle (M. pectoralis).
Journal of Food Engineering, 80(3), 813–821.
Gillespie, J., Nyaupane, N., & Boucher, R. (2012). Changes in crawfish production costs
and current production practices used. Aquaculture Economics & Management, 16(3),
250–265.
Harris, P., & Shorthose, W. (1988). Meat texture. In R. Lawrie (Ed.). Developments in meat
science (pp. 245–296). Elsevier Applied Science: London.
Herrera, J. J., Pastoriza, L., & Sampedro, G. (2001). A DSC study on the effects of various
maltodextrins and sucrose on protein changes in frozen-stored minced blue whiting
muscle. Journal of the Science of Food and Agriculture, 81(4), 377–384.
Hossan, M. R., Byun, D., & Dutta, P. (2010). Analysis of microwave heating for cylindrical
shaped objects. International Journal of Heat and Mass Transfer, 53(23), 5129–5138.
Ishiwatari, N., Fukuoka, M., & Sakai, N. (2013). Effect of protein denaturation degree on
texture and water state of cooked meat. Journal of Food Engineering, 117(3), 361–369.
Jouquand, C., Tessier, F. J., Bernard, J., Marier, D., Woodward, K., Jacolot, P., ...
Laguerre, J.-C. (2015). Optimization of microwave cooking of beef burgundy in terms
of nutritional and organoleptic properties. LWT - Food Science and Technology, 60(1),
271–276.
Kajitani, S., Fukuoka, M., & Sakai, N. (2011). Kinetics of thermal denaturation of protein
in cured pork meat. Japan Journal of Food Engineering, 12(1), 19–26.
Kong, F., Tang, J., Rasco, B., & Crapo, C. (2007). Kinetics of salmon quality changes
during thermal processing. Journal of Food Engineering, 83(4), 510–520.
Lefevre, F., Fauconneau, B., Thompson, J. W., & Gill, T. A. (2007). Thermal denaturation
and aggregation properties of Atlantic salmon myofibrils and myosin from white and
red muscles. Journal of Agricultural and Food Chemistry, 55(12), 4761–4770.
Li, M., Li, B., & Zhang, W. (2018). Rapid and non-invasive detection and imaging of the
hydrocolloid-injected prawns with low-field NMR and MRI. Food Chemistry, 242,
16–21.
Li, X., Llave, Y., Mao, W., Fukuoka, M., & Sakai, N. (2018). Heat and mass transfer,
shrinkage, and thermal protein denaturation of kuruma prawn (Marsupenaeus ja-
ponicas) during water bath treatment: A computational study with experimental
validation. Journal of Food Engineering, 238, 30–43.
Ling, B., Tang, J., Kong, F., Mitcham, E., & Wang, S. (2014). Kinetics of food quality
changes during thermal processing: A review. Food and Bioprocess Technology, 8,
343–358.
Liu, S., Yu, X., Fukuoka, M., & Sakai, N. (2014). Modeling of fish boiling under microwave
irradiation. Journal of Food Engineering, 140, 9–18.
Llave, Y., Matsuda, H., Fukuoka, M., & Sakai, N. (2014). Comparison of browning colour
formation on the surface of fish samples during grilling. Food Science and Technology
Research, 20(1), 85–91.
Llave, Y., Yu, X., Fukuoka, M., & Sakai, N. (2014). Analysis of the color developed during
carbonization of grilled fish by kinetics and computer imaging. Food Science and
Technology Research, 20(5), 1051–1061.
Mansfield, T. (1962). High temperature-short time sterilization. Proceedings of the 1st
International Congress on Food Science and Technology (pp. 311–316). Gordon and
Breach Science Publishers.
Mao, W., Li, X., Fukuoka, M., Liu, S., Ji, H., & Sakai, N. (2016). Study of Ca 2+-ATPase
activity and solubility in the whole Kuruma prawn (Marsupenaeus japonicus) meat
during heating: Based on the kinetics analysis of myofibril protein thermal dena-
turation. Food and Bioprocess Technology, 9(9), 1511–1520.
Matsuda, H., Llave, Y., Fukuoka, M., & Sakai, N. (2013). Color changes in fish during
grilling – Influences of heat transfer and heating medium on browning color. Journal
of Food Engineering, 116(1), 130–137.
Meullenet, J. F., Chang, H. C., Carpenter, J. A., & Resurreccion, A. V. A. (1994). Textural
properties of chicken frankfurters with added collagen fibers. Journal of Food Science,
59(4), 729–733.
Mochizuki, Y., Mizuno, H., Ogawa, H., & Iso, N. (1995). Trial determination of the ratio of
myosin and actin in raw meat by differential scanning calorimetry. Fisheries Science,
61(4), 723–724.
Moody, M. (1989). Processing of freshwater crawfish: A review. J. Shellfish Res, 8,
293–301.
Moore, L. J., Harrison, D. L., & Dayton, A. (1980). Differences among top round steaks
cooked by dry or moist heat in a conventional or a microwave oven. Journal of Food
Science, 45(4), 777–781.
Niamnuy, C., Devahastin, S., & Soponronnarit, S. (2008). Changes in protein compositions
and their effects on physical changes of shrimp during boiling in salt solution. Food
Chemistry, 108(1), 165–175.
Nunak, N., & Schleining, G. (2011). Instrumental textural changes in raw white shrimp
during iced storage. Journal of Aquatic Food Product Technology, 20(4), 350–360.
Rao, M. A., Rizvi, S. S., Datta, A. K., & Ahmed, J. (2014). Engineering properties of foods.
CRC press.
Robinson, G. W., Urquidi, J., Singh, S., & Cho, C. H. (2001). Protein denaturation de-
scribed by a two-state structural model of liquid water. Cellular and Molecular Biology
H. Fan, et al.
(Noisy-le-Grand, France), 47(5), 757–765.
Romero, A., Cordobés, F., Guerrero, A., & Puppo, M. C. (2011). Crayfish protein isolated
gels. A study of pH influence. Food Hydrocolloids, 25(6), 1490–1498.
Schubring, R. (2009). Comparative study of DSC pattern, colour and texture of shrimps
during heating. Journal of Thermal Analysis and Calorimetry, 95(3), 749.
Shao, Y., Xiong, G., Ling, J., Hu, Y., Shi, L., Qiao, Y., ... Wang, L. (2018). Effect of ultra-
high pressure treatment on shucking and meat properties of red swamp crayfish
(Procambarus clarkia). LWT, 87, 234–240.
Skipnes, D., Johnsen, O., Skara, T., Sivertsvik, M., & Lekang, O. (2011). Optimization of
heat processing of farmed Atlantic cod (Gadus morhua) muscle with respect to cook
loss, water holding capacity, color, and texture. Journal of Aquatic Food Product
Technology, 20(3), 331–340.
Sriket, P., Benjakul, S., Visessanguan, W., & Kijroongrojana, K. (2007). Comparative
studies on chemical composition and thermal properties of black tiger shrimp
(Penaeus monodon) and white shrimp (Penaeus vannamei) meats. Food Chemistry,
103(4), 1199–1207.
Tanaka, F., Mallikarjunan, P., & Hung, Y. C. (1999). Dielectric properties of shrimp re-
lated to microwave frequencies: From frozen to cooked stages. Journal of Food Process
Engineering, 22(6), 455–468.
Tornberg, E. (2005). Effects of heat on meat proteins – Implications on structure and
quality of meat products. Meat Science, 70(3), 493–508.
15
Innovative Food Science and Emerging Technologies 62 (2020) 102368
Uzzan, M., Kesselman, E., Ramon, O., Kopelman, I. J., & Mizrahi, S. (2006). Mechanism of
textural changes induced by microwave reheating of a surimi shrimp imitation.
Journal of Food Engineering, 74(2), 279–284.
Vadivambal, R., & Jayas, D. S. (2010). Non-uniform temperature distribution during
microwave heating of food materials—A review. Food and Bioprocess Technology,
3(2), 161–171.
Villota, R., & Hawkes, J. G. (2006). Reaction kinetics in food systems. Handbook of food
engineering (pp. 137–298). CRC Press.
Vittadini, E., Rinaldi, M., Chiavaro, E., Barbanti, D., & Massini, R. (2005). The effect of
different convection cooking methods on the instrumental quality and yield of pork
Longissimus dorsi. Meat Science, 69(4), 749–756.
Wang, J., Tang, J., Rasco, B., Sablani, S. S., Ovissipour, M., & Qu, Z. (2018). Kinetics of
quality changes of shrimp (Litopenaeus setiferus) during pasteurization. Food and
Bioprocess Technology, 11(5), 1027–1038.
Yang, H., Chen, Q., Cao, H., Fan, D., Huang, J., Zhao, J., ... Zhang, H. (2019).
Radiofrequency thawing of frozen minced fish based on the dielectric response me-
chanism. Innovative Food Science & Emerging Technologies, 52, 80–88.
Yu, X., Llave, Y., Fukuoka, M., & Sakai, N. (2014). Estimation of color changes in fish
surface at the beginning of grilling based on the degree of protein denaturation.
Journal of Food Engineering, 129, 12–20.