JFS: Food Chemistry and Toxicology

Milk Protein Coatings Prevent

Oxidative Browning of Apples and Potatoes
C. LE TIEN, C. VACHON, M.-A. MATEESCU, AND M. LACROIX

ABSTRACT: Color analysis on apple and potato slices coated with calcium caseinate or whey protein solutions
showed that the 2 coatings efficiently delayed browning by acting as oxygen barriers. The antioxidant properties of
Food Chemistry and Toxicology

the films were realized using a model allowing the release of oxidative species by electrolysis of saline buffer. Whey
proteins were a better antioxidant capacity than calcium caseinate. Furthermore, addition of carboxymethyl cellu-
lose (CMC) to the formulations significantly improved their antioxidative power. Best scavenging of oxygen free
radicals and reactive oxygen species was found for films based on whey proteins and CMC which inhibited by 75%
the formation of colored compounds produced by the reaction of the oxidative species with N,N-diethyl-p-phe-
nylenediamine.
Keywords : antioxidant; oxidative browning; edible coating; whey proteins; caseinate; color analysis.

Introduction tion on sliced mushrooms significantly reduced enzymatic

B ROWNING OF MANY FOOD PRODUCTS IS A MAJOR PROBLEM

for the food industry. The normal approach to inhibit
browning (Nisperos-Carriedo and others 1991).
This work reports color measurements, performed by
both enzymatic and nonenzymatic oxidative browning in trivariance analysis on sliced apples and potatoes coated
foods has been the application of sulfites. However, health with milk protein formulations, in order to determine effec-
concerns have limited their application (Sapers 1993). Other tiveness in postponing enzymatic browning. Furthermore,
techniques, including modified atmosphere packaging (MAP) antioxidant properties of films cast from whey and calcium
and vacuum packaging have been considered. While this ap- caseinate solutions were tested using the N,N-diethyl-p-phe-
proach can delay browning, excessive reduction of oxygen nylenediamine (DPD) colorimetric method.
will damage the product by inducing anaerobic metabolism,
leading to breakdown and off-flavor formation. Further- Materials and Methods
more, the removal of oxygen also entails a risk that anaero-
bic conditions in the product might become favorable for Materials
the growth of Clostridium botulinum (Sapers 1993). Another Calcium caseinate (Alanate 380) was provided by New
approach is the use of antibrowning agents based on citric Zealand Milk Products (Santa Rosa, Calif., U.S.A.). Concen-
acid or ascorbic acid. Although ascorbic acid can reduce en- trated whey protein powder was obtained from Saputo
zymatic browning, it can increase nonenzymatic browning Cheese Ltd. (St-Hyacinthe, Quebec, Canada). Glycerol
due to the its own oxidation into dehydroascorbic acid (99.5%, reagent grade) from American Chemicals Ltd.
(DHAA) which then reacts with amino acids to yield brown (Montreal, Quebec, Canada), carboxymethyl cellulose sodi-
colors by the Maillard reaction or other nonenzymatic pro- um salt (CMC, low viscosity) and N,N-diethyl-p-phenylenedi-
cesses (Kacem and others 1987). Furthermore, high concen- amine (DPD) from Sigma Chemical Co. (St. Louis, Mo.,
trations of acid or other chemical agents could significantly U.S.A.) were used as received, without further purification.
alter food flavor and odor. Recently, Sapers and others (1997)
showed that the use of harsh chemical treatments (heated Coating procedure and film formation
acid solutions) can induce severe textural damage in pre- a) Preparation of coating solution: Coating solutions were
peeled potatoes resulting in surface firming (case hardening) prepared with 5% protein (calcium caseinate or whey pro-
and separation of the superficial tissues that affect texture tein powder), 2.5% glycerol, 0.25% CMC, and 0.125% CaCl 2
after mashing and slicing following cooking. Such defects according to a method developed in our laboratory (Ressou-
would greatly limit the utilization of pre-peeled potatoes any and others 1998; Brault and others 1997). The compo-
which have received the antibrowning treatment. nents were mixed in distilled water to obtain homogeneous
Nussinovick and Kampf (1993), Hershko and Nussinovitch solution and heated at 80 8C for 30 min. The solutions were
(1998) proposed and used alginate-based coating solution to cooled at room temperature (20 6 1 8C) and the final solu-
conserve the mushroom for a long period with a better ap- tion pH was 6.5. Solutions were prepared immediately before
pearance and color. Tong and others (2000) showed that use and the color measurement was realized when the coat-
whey proteins are effective antioxidants in salmon oil-in-wa- ing solutions was applied on slices.
ter emulsions. The use of milk protein-based coatings, which McIntosh apples (Rougemont, Quebec, Canada) and Rus-
are flavorless, odorless, and edible, could also be beneficial set potatoes (Canada #1 from Prince Edward Island, Canada)
for controlling enzymatic browning of cut fruits and vegeta- were used. Five slices (each about 1 cm thick) were cut from
bles without inducing tissue damage. Edible coatings based 3 potatoes and 3 apples, dipped and held for 1 min in the
on cellulose gums have already been used to effectively delay coating solutions and laid on a flat surface for drying at
ripening in some climacteric fruits like mangoes, papayas, room temperature (20 6 1 8C). Control potatoes and apples
and bananas. Furthermore, application of the same formula- were cut and laid without dipping in the dishes and exposed

512 JOURNAL OF FOOD SCIENCE—Vol. 66, No. 4, 2001 © 2001 Institute of Food Technologists
Oxidative Browning of Apples and Potatoes . . .

to atmospheric air. The experiments were repeated 3 times.
(b) Preparation of film-forming solution: Films used for
measuring antioxidant properties were based on milk protein,
glycerol and CMC only. Solutions containing 5% protein (calci-
um caseinate or whey protein powder), 2.5% glycerol and with
or non 0.25% CMC were heated at 80 8C during 30 min. Heat
was essential for the formation of the intermolecular disulfide
bonds, this process is necessary to obtain a flexible film with
good mechanical properties (Vachon and others 2000; Le Tien
and others 2000). The reason for CMC addition resides in its
role as a matrix (protein stabilizing), whereas glycerol can play
the role of a plasticizer agent, which prevents breaking film
(Ressouany and others 1998). The solutions were cooled at
MgSO4 0.86 mM, CaCl2 1.25 mM, glucose 11.0 mM, and EDTA
0.06 mM). Preliminary results showed that similar oxidative
effect can be obtained by electrolysis of 0.15 M NaCl, in the
same conditions (10 mA, 400 V for 1 min).
The antioxidative capacity describes the film’s capacity to
inhibit the accumulation of oxidative species (able to oxidize
DPD) and the red coloration at 515 nm. The reaction is cali-
brated using the nonelectrolyzed KH buffer solution (no oxi-
dative species, ascribed to 100% scavenging) and the electro-
lyzed KH buffer solution (0% scavenging, in the absence of
any antioxidants). The scavenging percentage is calculated
following this equation:

Food Chemistry and Toxicology

room temperature (20 6 1 8C) and the final solution pH was
6.5. Films were cast by applying 5 mL of the solution onto a 8.5
cm diameter Petri dishes (Fisher Scientific, Montreal, Quebec,
Canada) and allowed to dry overnight at room temperature
(20 6 1 8C). Transparent dried films were peeled intact from
the casting surface and reconditioned in a desiccator contain-
ing a saturated NaBr solution, ensuring 56% relative humidity
(RH) at room temperature (20 6 1 8C), for at least 48 h (Gon-
tard and others 1992).
scavenging (%) = 100 – [ (OD sample /OD control) 3 100] (1)
where OD control represents the OD of electrolyzed solution
in the absence of film. In fact, OD is directly related to the
degree of oxidation of DPD reagent by the oxidative species.
Thus a film able to reduce completely the level of reactive
oxidative species will have a 100% scavenging capacity.
Results and Discussion

Color analysis and lightness evaluation

Color measurements were made at 5 min intervals for a
M ILK PROTEINS POSSESS NUMEROUS FUNCTIONAL PROPER-
ties which are important for the film formation (hydro-
gen, hydrophobic and ionic interactions). However, the heat-
total experimental period of 130 min. The color was evaluat- ing was necessary for the formation of the intermolecular
ed by trivariance analysis using a Colormet reflectance spec- disulfide bonds which improve the mechanical properties of
trocolorimeter (Instrumar Engineering Ltd., St. John’s, NF, film, particularly, the oxygen barrier (McHugh and Krochta
Canada) using the standard CIELAB (1976) color system. 1994). Addition of CMC in the formulation resides in its role
Lightness is reported as L* and the hue angle value is given as a matrix, whereas glycerol can play the role of a plasticiz-
by tan-1 (b*/a*). The lightness value for perfect white is 100, ing agent (Le Tien and others 2000). All milk protein-based
while L* = 0 corresponds to black. As the hue decreases, red films used in this experiment were transparent after com-
pigmentation increases. The a* axis (red) corresponds to a plete well drying.
hue angle of 0°. Color measurements were done on 15 slices
(potato or apple, n = 15). Coating and the oxidative browning
The variation of the lightness parameter (L*) as a function
Evaluation of antioxidant properties of time for coated potato slices is presented in Figure 1. For
Antioxidative capacities of film were evaluated following a the uncoated (control) slices, an increase in lightness was ob-
modified procedure of the DPD (N,N-diethyl-p-phenylenedi- served for the 1st 15 min. Then, L* value of the uncoated po-
amine) colorimetric method (APHA 1989), as reported by tato slices starts to progressively decrease with time for the re-
Dumoulin and others (1996). maining experimental period. Over the entire duration of the
(a) Film thickness measurement: Film thickness was mea-
sured using a Mitutoyo Digimatic Indicator (Mitutoyo, Tokyo,
Japan) at 5 random positions around the film. The average
film thickness was in the range of 50 6 5 mm and depended
upon the formulation.
(b) Antioxidative capacity determination: Films were cut
in pieces of equal thickness (50 6 4 mm), all measuring 0.8 3
2.5 cm (approximately 200 mg protein). They are then put in
a cell containing 3 mL of Krebs-Henseleit (KH) buffer and
submitted to electrolysis for 1 min (continuous current, 400
Volts; 10 mA) using a generator (Bio-Rad, model 1000/500).
After electrolysis, a volume of 200 mL of solution is sampled
and added to 2 mL of DPD solution (25 mg/mL). The oxida-
tive species react instantly with DPD producing a red colora-
tion that can be measured at 515 nm. The colorimetric reac-
tion was calibrated with potassium permanganate (KMnO 4)
solution. The oxidative capacity of 1.00 mg/L of free chlorine
solution (generating hypochlorous acid) corresponds to that
of 5.63 mmol/L KMnO4 solution.
Use of electrolysis as a method to generate oxidative
stress was first introduced by Jackson and others (1986) for
physiological studies on perfused isolated organs. Oxidative Figure 1—Time course of the lightness parameter (L*) for
damage was realized by electrolysis of KH buffer (NaCl 118.0 uncoated (control) and coated (calcium caseinate or whey
mM, NaHCO3 25.4 mM, KCl 4.8 mM, KH 2PO4 1.2 mM, protein) potato slices (n = 14; SD # 6 1.22)

Vol. 66, No. 4, 2001—JOURNAL OF FOOD SCIENCE 513

 Oxidative Browning of Apples and Potatoes . . .
experiment (130 min), the L* of the control slices varied from
70.64 (at t = 0) to 66.15 at (t = 130 min). The loss of lightness
can be estimated at 4.5% for the experimental period (130
min). Under the same conditions, the L* values observed for
coated potato slices did not show any evidence of loss of light-
ness. A slight increase in lightness was even noticed for all
types of coated potato slices between the 1st 45 min and 70
min respectively for calcium caseinate and whey proteins. Af-
ter 130 min, the lightness of the calcium caseinate-coated slic-
es was L* = 71.39 and a similar value (L* = 71.72) was noted for
the whey-coated slices. The increase of L* value in coated and
uncoated samples is probably due to the exudation of natural
liquid present in potato or the coating solution that contribute
Food Chemistry and Toxicology
to increase L* value. Afterward, L* value remained stable until
the end of the experiment.
Figure 2 shows the variation of hue angle for uncoated
and coated potato slices. As the hue angle decreases, red pig-
mentation becomes more pronounced. The control (uncoat-
ed) slices undergo rapid appearance of red pigmentation as
seen by the sharp decrease of the hue over the first 45 min.
Then, the hue was stable for the remainder of the experi-
mental period. For the coated slices (calcium caseinate and
whey proteins), only a slight variation of the hue was noticed
for the entire period of 130 min (Figure 1).
Figure 3 and 4 show the lightness (L*) and hue results ob-
tained for apple slices. Similar to the changes observed for po-
tato slices, L* rapidly decreased with time for the uncoated
apple slices (Figure 3). After 130 min, the average L* of the un-
coated apples was 66.11 compared to 74.77 at t = 0. This rep-
resents an overall lightness loss of more than 8% for the entire
period. For the coated apple slices, L* remained rather con-
stant showing that the protein coatings effectively protected
the fruit from oxygen. As for the hue (Figure 4), results show
that, for all apple slices, the angle decreased slightly with time.
The hue decrease was faster for uncoated slices and calcium
caseinate-treated slices. Best prevention was found with the
whey coating. Although the hue decreased, our data (Figure 3)
show that moderate color fluctuations were not associated
with darkening. Overall results clearly suggest that protein-
based edible coatings were successful in delaying oxidative
browning in sliced apples and potatoes.
Figure 2—Time course of the hue for uncoated (control)
and coated (calcium caseinate or whey protein) potato
slices (n = 15; SD # 6 1.58)
514 JOURNAL OF FOOD SCIENCE—Vol. 66, No. 4, 2001
Nisperos-Carriedo and others (1991) reported color mea-
surements done on sliced mushrooms coated with a formu-
lation containing vegetable oils, cellulose gums, emulsifiers,
surfactants, and fatty acids. They showed that the coating re-
duced enzymatic browning. After 2 h, the coated mush-
rooms were lighter than the uncoated ones. Still, the coating
did not completely inhibit darkening as the coated mush-
rooms were slightly darker after 2 h than the fresh-cut con-
trols. Milk protein-based formulations appeared more effec-
tive in controlling oxidative browning of sliced potatoes and
apples since color fluctuations were not enhanced by a lower
L* (Figure 1 and 3), even after 2 h.
A previous report showed that the addition of whey pow-
der improved the oxidative stability of soybean oil (Browdy
and Harris 1997). Protein coatings probably delay browning
by preventing the oxidative process. An important factor im-
plied in the inhibition of the oxidative browning is that the
coating by protein solution represents an efficient barrier to
oxygen (decreased oxygen penetration). However, this barri-
er is not total. Previous studies (McHugh and Krochta 1994)
demonstrated that these coatings are not completely imper-
vious to oxygen. Indeed, the oxygen permeability of milk
protein-based films were varied between 19 and 43 cm 3.ìm/
m2.d.kPa (25 8C). This feature would, consequently, lower the
risks of creating undesirable anaerobic conditions and re-
tarded oxidative browning. Other agents could also inhibit
enzymatic browning by different mechanisms. Many pro-
teins can exert certain antioxidative effects. The presence of
several side residues of amino acids, in particular, the cys-
teine in the milk proteins can directly or indirectly inhibit the
polyphenol oxidases. Dudley and Hotchkiss (1989) showed
that cysteine inhibits polyphenol oxidase via its SH groups,
acting as an agent coupling quinones and forming stable, col-
orless compounds. The same phenomenon has been ob-
served by Berlett and others 1997. Kohen and others (1988)
demonstrated that the histidine residues and its derivatives
(having an imidazole compound) possess an antioxidant ac-
tivity that was due to hydrogen donation. Indeed, the hydro-
gen on the ring nitrogen and on the methylene carbon next
to imidazol ring are likely donors. Furthermore, the enzyme
was also supposed to be competitively inhibited by the pres-
Figure 3—Time course of the lightness parameter (L*) for
uncoated (control) and coated (calcium caseinate or whey
protein) apple slices (n = 14; SD # 6 1.42)
Oxidative Browning of Apples and Potatoes . . .
ence of aromatic residues such as tyrosine, phenylalanine,
and tryptophan (Berlett and others 1997). Probably milk pro-
tein coatings exert prevention through both effects as barrier
limiting the access of oxygen and via a possible inhibitory ac-
tion at the level of polyphenol oxidases located in the tissues
cells. Additional effects could be related to the presence of
other components in the film formulation. For instance
CMC, as carbohydrate, can exert a nonspecific oxidative spe-
cies scavenging activity (Wehmeier and Mooradian 1994).
Another possible effect can be related to the carboxylic
groups of CMC which, in certain conditions as a chelating
agent, can interact with the copper binding site for the oxy-
gen and decrease polyphenol oxidases activity (Sapers 1993).
Hershko and Nussinovitch (1998) showed that alginate-based
coating solution, a carbohydrate having a carboxylic group,
allowed to conserve the mushroom for a long period with a
better appearance and color. In addition, our results indicat-
ed that the best prevention was found with the whey coating.
This could be due to the presence of fatty acids (5.4% in the
whey protein) that significantly improved the moisture barri-
er properties and significantly reduced browning in fresh-cut
Figure 4—Time course of the hue for uncoated (control)
and coated (calcium caseinate or whey protein) apple
slices (n = 15; SD # 6 1.29)
Figure 5—Antioxidant capacity (%) for film formulations
based on calcium caseinate or whey proteins with or with-
out CMC.
apples (McHugh and Senesi 2000). In order to further evalu-
ate the antioxidant capacities of these films, measurements
were carried out using a model allowing the release of reac-
tive oxidative species by electrolysis of saline buffer.
Antioxidant properties of protein films
The antioxidative power of protein films is presented in Fig-
ure 5. Milk protein films containing CMC had better antioxida-
tive capacities than those based only on protein (caseinate or
whey) and glycerol. The antioxidant capacities of milk protein-
glycerol films were 37.63% for the calcium caseinate and 60.21%
for whey protein films. When CMC was added to the film for-
mulations, the antioxidant capacities increased to 66.14 % for
Food Chemistry and Toxicology
calcium caseinate (Alanate) and to 75.17% for whey. It can be
seen that for both types of formulations, whey proteins exhibit
a higher antioxidative power than calcium caseinate. Further-
more, the addition of CMC increased the antioxidative power of
these films by 43% for the calcium caseinate formulations and
by 20% for the whey protein formulations.
Many factors could account for the antioxidative proper-
ties of milk protein films. In addition to cysteine, aromatic
amino acids like tyrosine, tryptophan and histidine are po-
tent free radical targets (Berlett and Stadtman 1997). Fur-
thermore, Colbert and Decker (1991) reported that the anti-
oxidative activity of acid whey was related to a low-molecu-
lar-weight fraction (500-5000 Da). This observation is possi-
bly related to smaller peptides. Several peptides such as car-
nosine and anserine have shown a great antioxidative effect
(Kohen and others 1988). The higher antioxidative potential
of whey proteins compared to calcium caseinate could be
due to the presence of lactose. Indeed, the commercial whey
protein used contained 14% lactose, which is known for its
free radical scavenging effects (Wehmeier and Mooradian
1994). In addition, Xue and others (1998) showed that algi-
nate and carboxymethyl chitosan retarded the hydroperox-
ide accumulation of methyl linoleate by effectively trapping
peroxide radicals. Similarly, the addition of a polysaccharide
like CMC can probably also increase the antioxidative activity
of these formulations.
Conclusion
T HIS REPORT SHOWED THE EFFECT OF MILK PROTEIN-BASED
edible coatings on the browning reaction of sliced apples
and potatoes. Results confirm that the formulations were ef-
fective in delaying browning reactions by acting as oxygen
barriers and/or reactive oxidative species scavengers. Fur-
thermore, an electrolysis model generating oxidative species
was used to assess the antioxidative potential of these films.
Whey was shown to be a better antioxidant than calcium
caseinate. Such differences can be explained by the varia-
tions in amino acid composition in the 2 types of protein.
Furthermore, lactose, which is present in commercial whey,
can also account for the increased antioxidative activity; sim-
ple sugars are known for their free radical quenching effect.
Similarly, the addition of a polysaccharide, like CMC, can fur-
ther increase the antioxidative potential of our film formula-
tions.
The use of milk proteins as natural antioxidants is a
promising development in related fields of food science.
The proteins are flavorless, odorless, and edible, and could
be beneficial for controlling enzymatic browning of cut
fruits and vegetables without inducing tissue damage. Milk
proteins represent interesting agents to be used in some
processed foods to prevent the formation of hydroperox-
ides and lipid peroxidation.
Vol. 66, No. 4, 2001—JOURNAL OF FOOD SCIENCE 515
 Oxidative Browning of Apples and Potatoes . . .
References
APHA. 1989. DPD colorimetric method. Standard method for the examination of
water and wastewater. 17 th edition, Washington DC: American Public Health
Association. 4-(62-64).
Berlett BS, Stadtman ER. 1997 Protein oxidation in aging, disease and oxidative
stress. J Biol Chem 272 (33): 20313-20316.
Brault D, D’Aprano G, Lacroix M. 1997. Formation of free-standing sterilized
edible films from irradiated caseinates. J Agric Food Chem 45 (8): 2964-2969.
Browdy AA, Harris ND. 1997 Whey improves oxidative stability of soybean oil. J
Food Sci 62 (2): 348-376.
CIELAB. 1976. Color space adapted by CIE in 1974 with recommendations for
associated psychometric color terms at the International Commissions on Il-
luminations (CIE, 1974). Method of measuring and specifying color rendering
properties of light sources, Publication CIE N° 13-2 (TC.3.2) Paris: Bureau cen-
tral de la CIE, 1976.
Colbert LB, Decker EA. 1991. Antioxidant activity of an ultrafiltration permeate
from acid whey. J Food Sci 56 (5): 1248-1250.
Dudley ED, Hotchkiss JH. 1989. Cysteine as an inhibitor of polyphenol oxidase.
Food Chemistry and Toxicology
J Food Biochem 13 (1): 65-75.
Duckwork HW, Coleman JE. 1970. Physicochemical and kinetic properties of
mushroom tyrosinase. J Biol Chem 245 (7): 1613-1625.
Dumoulin M J, Chahine R, Atanasiu R, Nadeau R, Mateescu MA. 1996. Compara-
tive antioxidant and cardioprotective effects of ceruloplasmin, superoxide
dismutase and albumin. Arzneim.-Forsch./Drug Res 46 (9): 855-861.
Gontard, N, Guilbert, S, CuQ JL. 1992. Edible Wheat gluten films: influence of the
main process variables on film properties using response surface methodol-
ogy. J Food Sci 57 (1): 190-199.
Hershko V, Nussinovitch A. 1998. Relationships between hydrocolloid coating
and mushroom structure. J Agric Food Chem 46 (8): 2988-2997
Jackson CV, Mickelson JK, Stringer K, Rao PS, Lucchesi BR. 1986. Electrolysis –
induced myocardial dysfunction. A novel method for the study of free radical
mediated tissue injury. J Pharmacol Methods 15 (4): 305-320.
Kacem B, Cornell JA, Marshall M.R, Shireman RB, Matthews RF. 1987. Nonenzy-
matic browning in aseptically packaged orange drinks: Effect of ascorbic acid,
amino acids and oxygen. J Food Sci 52 (6): 1668-1672.
Kohen R, Yamamoto Y, Cundry KC, Ames BN. 1988. Antioxidant activity of carnos-
ine, homocarnosine and anserine present in muscle and brain. Proc Natl Acad
Sci 85 (9): 3175-3179.
Le Tien C, Letendre M, Ispas-Szabo P, Mateescu MA, Delmas-Patterson G, Yu HL,
516 JOURNAL OF FOOD SCIENCE—Vol. 66, No. 4, 2001
Lacroix M. 2000. Development of biodegradable films from whey proteins by
cross-linking and entrapment in cellulose. J Agric Food Chem 48 (11): 5566-
5575.
McHugh TH, Krochta JM. 1994. Milk-protein-based edible films and coatings.
Food Technol 48 (1): 97-103.
McHugh TH, Senesi E. 2000. Apple Wraps: A novel method to improve the quality
and extend the shelf life of fresh-cut apples. J Food Sci 65 (3): 480-485.
Nisperos-Carriedo MO, Baldwin EA, Shaw PE. 1991. Development of an edible
coating for extending postharvest life of selected fruits and vegetables. Proc
Florida State Hort Soc, No. 104, 122-125.
Nussinovitch A, Kampf N. 1993. Shelf life extension and conserved texture of
alginated coated mushrooms (Agaricus bisporus). J Food Technol 26: 469-475.
Ressouany M, Vachon C, Lacroix M. 1998. Irradiation dose and calcium effect of
the chemical properties of cross-linked caseinate films. J Agric Food Chem 46
(4): 1618-1623.
Sapers GM. 1993. Browning of foods: Control by sulfites, antioxidants and other
means. Food Technol 47 (10): 75-84.
Sapers GM, Cooke PH, Heidel AE, Martin ST, Miller RL. 1997. Structural changes
related to texture of pre-peeled potatoes. J Food Sci 62 (4): 797-803.
Tong L M, Sasakis S, Mc Clements DJ and Decker EA. 2000. Antioxydant activity
of whey in a salmon oil emulsion. J Food Sci 65 (8): 1325-1329.
Vachon C, Yu H L, Yefsah R, Alain R, St-Gelais D and Lacroix M. 2000. Mechanical
and structural properties of milk protein edible films cross-linked by heating
and irradiation. J Agric Food Chem 48 (8): 559-566.
Wehmeier K.R, Mooradian A.D. 1994. Autoxidative and antioxidative potential of
simple carbohydrates. Free Radic Biol Med 17 (1): 83-86.
Xue C, YU G, Hirata T, Terao J, LIN H. 1998. Antioxidative activities of several
marine polysaccharides evaluated in a phosphatidylcholine-liposomal sus-
pension and organic solvents. Biosci Biotechnol Biochem 62 (2): 206-209
MS 20000228
This work was funded by the FCAR-Novalait and CQVB program. A NSERC graduate
studentship granted to C. Le Tien and an Institut Armand-Frappier postdoctoral fellowship
granted to C. Vachon are gratefully acknowledged. The authors also thank Michèle Jobin
for her collaboration.
Authors Le Tein, Vachon, and Lacroix are associated with INRS-Institut
Armand Frappier, Laval, Canada, and author Mateescu is associated with
the University of Quebec. Please address correspondence to Author Lacroix
(E-mail: Monique_Lacroix@inrs-iaf.uquebec.ca)