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Rieny Sulistijowati Chitinase Activity Potential and Identification of Chitinolytic Bacteria Isolated of Swimmer Crabs Cell
Rieny Sulistijowati Chitinase Activity Potential and Identification of Chitinolytic Bacteria Isolated of Swimmer Crabs Cell
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International Journal of Agricultural and Biological Engineering (IJABE, https://www.ijabe.org) is a peer reviewed open
access international journal. IJABE, started in 2008, is a joint publication co-sponsored by US-based Association of
Agricultural, Biological and Food Engineers (AOCABFE) and China-based Chinese Society of Agricultural Engineering
(CSAE). The ISSN 1934-6344 and eISSN 1934-6352 numbers for both print and online IJABE have been registered in US.
Now, Int. J. Agric. & Biol. Eng (IJABE) is published in both online and print version by Chinese Academy of Agricultural
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International Journal of Agricultural and Biological Engineering (IJABE, https://www.ijabe.org) is a peer reviewed open
access international journal. IJABE, started in 2008, is a joint publication co-sponsored by US-based Association of
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(CSAE). The ISSN 1934-6344 and eISSN 1934-6352 numbers for both print and online IJABE have been registered in
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IJABE JIF=1.731, ranking 6 out of 13, locating Q2 according to JCR2019.
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Chitinase activity potential and identification of chitinolytic bacteria isolated of swimmer crab’s PDF
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Chitinase activity potential and identification of chitinolytic bacteria Search
isolated of swimmer crab’s cell
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Rieny Sulistijowati, . Sudin, Rita Marsuci Harmain
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This study aimed at investigating the chitinase enzyme activity produced by chitinolytic bacteria from the skin of blue By Issue
By Author
swimmer crab (Portunus pelagicus) and identification of the genus isolate. This study consists of two stages: firstly, the
By Title
qualitative and quantitative activity of the chitinase enzyme; and secondly, biochemical identification of the bacteria.
The quantitative chitinase enzyme activity is measured using the UV-Vis spectrophotometer UV-Vis at the wavelength
at 660 nm. The chitinase enzyme is obtained from the isolation of chitinolytic bacteria cultured within a media to grow
solid chitin, which contains colloidal chitin substrate as chitinase inductor at the temperature of 30°C. The highest DONATIONS
chitinolytic activity is obtained from the 24 h supernatant culture, with a value of enzyme activity at 0.149 U/mL.
Macroscopic and microscopic identification showed that the chitinolytic bacteria isolate R1, whereas the biochemical cell
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shows the characteristics of the genus Pseudomonas.
Keywords: biodegradable, chitinase, spectrophotometer, Portunus pelagicus, Pseudomonas
DOI: 10.25165/j.ijabe.20211403.5273
Citation: Sulistijowati R, Sudin, Harmain R M. Chitinase activity potential and identification of chitinolytic bacteria INFORMATION
isolated of swimmer crab’s cell. Int J Agric & Biol Eng, 2021; 14(3): 228–231. For Readers
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biodegradable, chitinase, spectrophotometer, Portunus pelagicus, Pseudomonas
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References
[References]
Bhattacharya D, Nagpure A, Gupta K R. Bacterial chitinases: Properties and potential. Critical Reviews in
Biotechnology, 2008; 27(1): 21–28.
Younes I, Bellaaj O G, Nasri R, Chaabouni M, Rinaudo M, Nasri M. Chitin and chitosan preparation from shrimp shells
using optimized enzymatic deproteinization. Journal Process Chemistry, 2012; 47: 2032–2039.
Arbia W, Arbia L, Adour L, Amrane A. Chitin extraction from crustaceanshells using biological methods. A Review Food
Technol
Purkan P, Baktir A, Sayyidah A R. Production of chitinase enzyme from aspergillus niger utilizing the blue swimmer
crab’s waste as inducer/ Produksi enzim kitinase dari Aspergillus niger menggunakan limbah cangkang rajungan
sebagai induser. Journal Kimia Riset, 2016; 1(1): 34–38. (in Indonesian)
Oh Y S, Shih L, Tzeng Y M, Wang S L. Protease produced by Pseudomonas aeruginosa K-187 and its application in the
deproteinization of shrimp and crab shell waste. Enzyme and Microbial Technology, 2000; 27(1-2): 3–10.
Homaei A, Lavajoo F, Sariri R. Development of marine biotechnology as a resource for novel proteases and their role in
modern biotechnology. International Journal of Biological Macromolecules, 2016; 88: 542–552.
Sudin, Sulistijowati R, Harmain R M. Screening and growth pattern chitinolytic bacteria of blue swimmer crab’s cell/
Penapisan dan pola pertumbuhan bakteri kitinolitik dari cangkang rajungan. Jambura Fish Processing Journal, 2020;
2(1): 36–45. (in Indonesian)
Purkan P, Azizah B, Baktir A, Sumarsih S. Exploration of chitinolytic bacteria from organic waste: Isolation and
characterization of chitinase enzyme. Journal of Molecular, 2014; 9(2): 129–133.
Cappuccino J G, Sherman N. Microbiology a laboratory manual. Seven Edition. State University of New York, 2005;
143–203.
Aditi F Y, Rahman S S, Hossain M D M. A study on the microbiological status of mineral drinking water. The Open
Microbiology Journal 2017; 11: 31–34.
Patil R S, Ghormade V, Despande M V. Chitinolytic enzymes: An exploration. Journal Enzyme and Microbial Technology,
2000; 26: 473–483.
Fukamizo T. Chitinolytic enzyme: Catalysis, substrate binding, and their application. Journal Current Protein & Peptide
Science, 2000; 1(1): 105–124.
Orinda E, Puspita I D, Putra M P, Ustadi U, Lelana, I Y B. Chitinolytic enzyme activity of isolate SDI23 from petis and
the activity of its partially purified enzyme in different pH and temperature (Aktivitas enzim pendegradasi kitin dari
isolat SDI23 asal petis serta karakterisasi ph dan suhu dan aktivitas enzim hasil purivikasi parsial. Jurnal Perikanan). J.
Fish. Sci, 2015; 17(2): 96–102. (in Indonesian)
Zhu M M, He H J, Fan M T, Ma H J, Ren H W, Zeng J, et al. Application and optimization of solid-state fermentation
process for enhancing polygalacturonase production by Penicillium expansum. Int J Agri & Biol Eng, 2018; 11(6): 187–
194.
Setia I N, Suharjono. Chitinolytic assay and identification of bacteria Isolated from shrimp waste based on 16S rDNA
sequences. Advances in Microbiology, 2015; 5: 541–548.
Hemraj V, Dikhsa S, Afneet G. A review commonly used biochemical test for bacteria. Journal of Life Science, 2013;
1(1): 1–7.
Amano M M T, Enokimoto M, Yano T, Moe K K, Misawa N. Influence of pH of TSI medium on the detection of hydrogen
sulfide production by campylobacter hyointestinalis. Journal Compilation, 2007; 44: 544–549.
Cowan S C, Steel S. Manual for the identification of medical bacteria. Cambridge University Press Cambridge, London,
2003.
Wang S L, Chang W T. Purification and characterization of two bifunctional chitinases/lysozymes extracellularly
produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. Applied and Environmental
Microbiology, 1997: 63(2): 380–386.
Thomson S E, Smith M, Wilkinson M C, Peek K. Identification and characterization of chitinase antigen from
Pseudomonas aeruginosa strain 385. Applied and Environmental Microbiology, 2001; 67(9): 4001–4008.
This work is licensed under a Creative Commons Attribution 4.0 International License.
Abstract: This study aimed at investigating the chitinase enzyme activity produced by chitinolytic bacteria from the skin of
blue swimmer crab (Portunus pelagicus) and identification of the genus isolate. This study consists of two stages: firstly, the
qualitative and quantitative activity of the chitinase enzyme; and secondly, biochemical identification of the bacteria. The
quantitative chitinase enzyme activity is measured using the UV-Vis spectrophotometer UV-Vis at the wavelength at 660 nm.
The chitinase enzyme is obtained from the isolation of chitinolytic bacteria cultured within a media to grow solid chitin, which
contains colloidal chitin substrate as chitinase inductor at the temperature of 30°C. The highest chitinolytic activity is
obtained from the 24 h supernatant culture, with a value of enzyme activity at 0.149 U/mL. Macroscopic and microscopic
identification showed that the chitinolytic bacteria isolate R1, whereas the biochemical cell shows the characteristics of the
genus Pseudomonas.
Keywords: biodegradable, chitinase, spectrophotometer, Portunus pelagicus, Pseudomonas
DOI: 10.25165/j.ijabe.20211403.5273
Citation: Sulistijowati R, Sudin, Harmain R M. Chitinase activity potential and identification of chitinolytic bacteria isolated
of swimmer crab’s cell. Int J Agric & Biol Eng, 2021; 14(3): 228–231.
This is due to the type of bacteria growth pattern and enzyme to produce H2S which signified by the existence of black sediment
activity needs to be known to have a good degrading ability. was observed; Oxidation/fermentation (O/F) test was inoculating
Therefore, this study aimed at testing the produced chitinase the bacteria into the O/F medium, which incubated for 24 h in the
activity and identification chitinase producer bacteria of blue temperature of 30°C, then observe the ability of the bacteria to use
swimmer crab. carbohydrate through fermentation or oxidation; TSIA (triple sugar
iron agar) test was inoculating bacteria into TSIA media, which
2 Methods and materials incubated for 24-48 h in the temperature of 30°C, then the ability of
2.1 Station and laboratory the bacteria in fermenting glucose, lactose, and sucrose was
Isolate R1 was obtained from fresh blue swimmer crab’s cells observed; Indole test was inoculating bacteria into indole media,
which came from the crabs’ farmer in Katialada village of which incubated for 24 h in the temperature of 30°C, then the
Kwandang sub-district of North Gorontalo Regency, Gorontalo ability of bacteria in degrading the tryptophan amino acid in the
Province of Indonesia. The identification biochemical test of the medium was observed.
chitinolytic bacteria were carried out at the Fish Quarantine Station
3 Results and discussion
Laboratory Quality Control and Fisheries Product Security Class I
Gorontalo Province of Indonesia, and the chitinolytic bacteria 3.1 Quantitative activity of the chitinolytic bacteria enzyme
enzyme activity test are carried out at the Pharmaceutical The activity of the chitinolytic bacteria enzyme is essential to
Laboratory of Universitas Negeri Gorontalo. be known to find out the ability of the bacteria to produce the
2.2 Materials enzyme in 33 h with an interval of 3 h. As shown in Figure 1,
The tools used in this study were test tube, inoculum needle, there were several increasing and decreasing stages in chitinase
vortex, measuring cup, beaker glass, Erlenmeyer, centrifuge, activity. The first inclination happened during the incubation time
centrifuge tube, shaker, pH meter, micropipette, micro tip, stirrer, of 0 to 12 h. The second increase of the enzyme activity showed
magnetic stabilizer, petri dish, oven, crooked spoon, Bunsen lamp, that the substrate was starting to be hydrolyzed to produce the
incubator, laminar air, analytical scales, UV-vis spectrophotometer, chitinase enzyme. Hence, bacteria could digest nutrition. Patil
and microscope. et al.[11] found that bacteria produce extracellular chitinase to take
Materials used in this study were R1 isolated of blue swimmer on nutrition. Following this inclination, there is the first declining
crab’s cell, chitin, chitin colloidal (chitin, condensed HCl, NaOH, phase on the 15th to the 18th hour of incubation. The decrease of
distillate water), chitin agar (chitin colloidal, KH2PO4, this enzyme activity is due to other compounds (aside from N-Acetyl
MgSO4·7H2O, yeast extract, agar, distillate water), Luria broth glucosamine) that triggers the decrease of enzyme production.
(yeast extract, tryptone water, NaCl, distillate water), nutrient agar,
aluminum foil, alcohol, crystal violet, iodine solution, glucose,
sucrose, lactose, maltose, mannitol, triple sugar iron agar, motility
indole ornithine, oxidative/fermentative, methyl red-Voges
Proskauer, methyl-red, and sterile liquid paraffin.
2.3 Quantitative activity of chitinase enzyme test
One dose of inoculum was added into 100 mL of production
medium (similar composition to a solid medium, but without agar)
then incubated in the temperature of 30°C and centrifuged in the
speed of 170 r/min. Every three hours, 2 mL of cell culture was
sampled for 33 h. Then centrifuged in the temperature of 4°C using
Figure 1 Chitinase activity curve from Pseudomonas
10.000 r/min speed for 10 min, the formed supernatant was the raw
extract of chitinase enzyme. The absorbance is then measured This phenomenon is due to the existence of other chitin-degrading
using spectrophotometer UV/Vis in wavelength of 660 nm[8], the enzymes produced by the bacteria. Colloidal chitin also can be
sample was carried out twice repetitions. hydrolyzed by deacetylating chitin produced by chitosan and
2.4 Biochemical test chitosanase which produce chitobiose[12]. Following this
The biochemical test was carried out to identify and classify declining phase, the chitinase activity climbs up in the incubation
bacteria into their group of taxonomy. The principle of this time of the 21st hour to its highest chitinase activity can be obtained
biochemical test is that if the bacteria are cultured in several media, from the supernatant culture in the incubation of time of the 24th
the bacteria show macroscopic differences in their growth[9,10]. hour, which stated with the value of enzyme activity of 0.149 U/mL.
Carbohydrate fermentation test was to find out the bacteria’s ability One unit of chitinase enzyme activity is defined as several enzymes
in fermenting carbohydrate by preparing the carbohydrate broth needed to release 1 mmol NAG/min. This result is different from
which consists of glucose, sucrose, maltose, and mannitol; MR-VP the result of the enzymes activity test carried out by Purkan et al.[8]
(methyl red-Voges Proskauer) test was to inoculate bacteria into a who found that the highest enzyme activity was in the 18th hour of
medium, which incubated in the temperature of 30°C for 24 h by incubation time, which stated with the value of enzyme activity of
adding methyl red reagent and KOH, to observe the bacteria ability 0.3850 U/mL. Moreover the ability of the bacteria to produce
in producing the mix acid and acetylenes; Citrate test was chitinase highly varied. Factors such as different types of bacteria,
inoculating bacteria into a medium and incubated in the the growth rate of each isolate in the medium, temperature, pH or
temperature of 30°C for 24 h by adding bromothymol blue (BTB) laboratory treatment during the experiment can be factors that
reagent, then the ability of the bacteria to use citrate as the only influence variation in the produced enzyme activity[13,14].
source of carbon was observed; H2S test was to inoculate the Chitinase activity was 0.213 and 0.219 U/mL respectively of PBK 2
bacteria into sulfide indole motility (SIM) which incubated for and SA 1.2 isolates from shrimp waste. Based on 16S rDNA
24-48 h in the temperature of 30°C, then the ability of the bacteria sequences, isolate of PBK 2 was identified as Acinetobacter
230 May, 2021 Int J Agric & Biol Eng Open Access at https://www.ijabe.org Vol. 14 No. 3
johnsonii 3-1, whereas SA 1.2 was identified as Bacillus Table 1 Biochemical characteristics of chitinolytic bacteria
amyloliquefaciens GR53 with 99.78% similarity[15]. isolate R1
The rebound of enzyme activity shows that there is more of the No Test Results
substrate being hydrolyzed. The chitinase enzyme activity is
1 Glucose fermentation Negative
steadily increasing until it reaches optimum incubation time.
2 Sucrose fermentation Negative
Following the reach of this optimum incubation time, the enzyme
3 Lactose fermentation Negative
activity decreases due to the accumulation of hydrolyzed products,
4 Maltose fermentation Negative
which can further inhibit the enzyme activity. This is
5 Mannitol fermentation Negative
characterized by the decrease of enzyme activity on the incubation
6 Citrate use Negative
time of hour 27 to hour 33. The decrease of chitinase enzyme
7 Sulfide indole motility Negative
activity after the optimum incubation time is due to the changes in
8 Triple sugar iron agar Alkaline/Alkaline
the state of the enzyme ion and the state of substrate ion which
9 Methyl red reaction Negative
caused denaturation of enzyme which followed by the loose of
10 Voges Proskauer reaction Negative
enzyme catalytic activity[12]. Besides, there are also change in the
11 Indole production Negative
tertiary structure of the enzyme due to denaturation, which made
12 Oxidase/Fermentative action Negative
the hydrophobic amino acid group within the enzyme come into
contact with water, thus, the solubility of the enzyme weakens. Fermentation test in several types of carbohydrate (glucose,
The decrease of chitinase solubility causes a gradual decrease in maltose, sucrose, mannitol, lactose) shows that all fermentation
enzyme activity. reaction is negative. This is characterized by the unchanging red
Chitinolytic bacteria isolates showed unstable chitinase activity color of the carbohydrate media. When the color of the medium
(fluctuate). This may be due to the isolate that produces the in the carbohydrate test turns into yellow, it means that the colony
chitinase at the beginning of its growth[13]. In line with the forms acid from that carbohydrate[10].
utilization of nutrition for growth, it is also suspected that chitinase A citrate test was carried out to find out the ability of the
is also used by bacteria as a source of protein, thus its chitinase chitinolytic bacteria isolates to utilize citrate as the only source of
activity decreases. carbon and energy. When a microorganism can use citrate, there
The decrease of enzyme activity can also be caused by factors will be an increase of pH and change in the color of the media into
such as temperature, pH, substrate and biomass during treatment in blue color. In this study, the citrate test reveals that the chitinolytic
the laboratory. The temperature has two main influences on the bacteria cannot utilize citrate as the only source of carbon. This is
reaction and the denaturation. The influence of reaction toward the shown by the unchanging green color of the media, which means
enzyme is that the increase of temperature will accelerate the that the test result is negative. Positive test results in the citrate test
reaction process, while the decrease in the temperature will cause are shown when the color changes from green to blue[16].
the reaction to slow down. When the temperature reaches a certain Further, the H2S test result in SIM is negative. This negative
limit, it will cause denaturation. Besides, when the pH of the result is reached when microorganism has no ability to hydrolyzed
environment is too acid or base, enzyme denaturation can also heavy metal within the media. H2S is produced by several types
happen. Reaction speed catalyzed by the enzyme is highly of microorganisms, which can break or degrade amino acid within
influenced by substrate concentration. In the low level of the sulfur (S). The existence of H2S can be observed by adding
substrate concentration, reaction speed by catalyzed by the enzyme several crystals of heavy metals into the media.
can also be very low. In reverse, reaction speed will increase along The reaction observable in the TSIA test shows a red color,
with the increase of substrate concentrate up to certain points that is which means that there is no change of color in both vertical and
the maximum reaction speed limit. When this saturated point of slight agar. This indicates that the bacteria are unable to ferment
the enzyme has been reached, it will not function properly. Lastly, sugar. In the vertical agar if the bacteria can ferment glucose, the
the number of bacteria inoculum (biomass) inserted into the media color of the media will change from red to yellow[17]. Whereas in
also strongly influence the enzyme activity. slight agar, if the bacteria can ferment lactose and sucrose, the
3.2 Biochemical test color of the media will change into yellow, meanwhile, when there
The biochemical test toward the characteristics of chitinolytic is no fermentation process of lactose and sucrose, the color will not
bacteria was carried out by fermenting bacteria in the various change.
sources of nutrition as shown in Figure 2. The biochemical test Methyl red test also reveals a negative result. This is shown
result of chitinolytic bacteria is presented in Table 1. by the unchanging color of the media which does not change into
yellow even after the addition of methyl red reagent. The red
colour signifies the positive test result, and if the color of the broth
is yellow, then the result of the test is negative[16]. Similarly, the
Voges Proskauer test also shows a negative result. This is evident
after the addition of the KOH solution; the color does not change.
The Voges Proskauer test will be stated as positive when there is a
form of acid, which signifies by the changes of medium color into
pink after the KOH solution is added. Meanwhile, the indole test
also shows a negative result. This result is obtained after the
reagent Kovac is added, which signify by the formation of a yellow
ring. The existence of indole is detected by Kovac reagent and the
Figure 2 Isolate R1 (10×100 magnification) formation of a red ring.
May, 2021 Sulistijowati R, et al. Chitinase activity potential and identification of chitinolytic bacteria isolated of swimmer crab’s cell Vol. 14 No.3 231
The objective of the oxidizing fermentative test is to find out Biotechnol, 2013; 51(1): 12–25.
the oxidation and fermentation characteristics of bacteria toward [4] Purkan P, Baktir A, Sayyidah A R. Production of chitinase enzyme from
aspergillus niger utilizing the blue swimmer crab’s waste as inducer/
glucose. Based on the result of the study on the O/F test, it does Produksi enzim kitinase dari Aspergillus niger menggunakan limbah
not show either oxidation or fermentation. This is evident when cangkang rajungan sebagai induser. Journal Kimia Riset, 2016; 1(1):
the media, either without liquid paraffin or without paraffin at all, 34–38. (in Indonesian)
do not change color. Bacteria are said to be fermentative when [5] Oh Y S, Shih L, Tzeng Y M, Wang S L. Protease produced by
Pseudomonas aeruginosa K-187 and its application in the deproteinization
both inoculated media change color into yellow. Bacteria are
of shrimp and crab shell waste. Enzyme and Microbial Technology, 2000;
oxidative when tube sealed with no paraffin changes color into 27(1-2): 3–10.
yellow and the tube sealed with paraffin does not change color[18]. [6] Homaei A, Lavajoo F, Sariri R. Development of marine biotechnology as
The morphology test result (macroscopic and microscopic tests) a resource for novel proteases and their role in modern biotechnology.
of chitinolytic bacteria have bar cell and gram-negative[9]. The International Journal of Biological Macromolecules, 2016; 88: 542–552.
[7] Sudin, Sulistijowati R, Harmain R M. Screening and growth pattern
biochemical test of the chitinolytic bacteria consists of chitinolytic bacteria of blue swimmer crab’s cell/ Penapisan dan pola
carbohydrate, citrate, sulfide indole motility, triple sugar iron agar, pertumbuhan bakteri kitinolitik dari cangkang rajungan. Jambura Fish
MR-VP, indole and O/F test should obtain negative results as Processing Journal, 2020; 2(1): 36–45. (in Indonesian)
indicators of a genus of Pseudomonas. Several studies to [8] Purkan P, Azizah B, Baktir A, Sumarsih S. Exploration of chitinolytic
bacteria from organic waste: Isolation and characterization of chitinase
determine chitinolytic bacteria from the genus of Pseudomonas[4]
enzyme. Journal of Molecular, 2014; 9(2): 129–133.
that utilized blue swimmer crab’s waste as an inducer to the [9] Cappuccino J G, Sherman N. Microbiology a laboratory manual. Seven
production of chitinase enzyme from Aspergillus niger. A study Edition. State University of New York, 2005; 143–203.
by Arbia et al.[3] isolated chitinolytic bacteria to produce several [10] Aditi F Y, Rahman S S, Hossain M D M. A study on the microbiological
status of mineral drinking water. The Open Microbiology Journal 2017;
bacteria, one of which was Pseudomonas aeruginosa bacteria
11: 31–34.
isolated from crab’s cell. Genus Pseudomonas generally has bar [11] Patil R S, Ghormade V, Despande M V. Chitinolytic enzymes: An
cell shape and gram-negative. A study by Wang et al.[19] isolated exploration. Journal Enzyme and Microbial Technology, 2000; 26: 473–483.
Pseudomonas aeruginosa K-187 known produced two bifungtional [12] Fukamizo T. Chitinolytic enzyme: Catalysis, substrate binding, and their
chitinase and lysozyme. Thompson et al.[20] found that application. Journal Current Protein & Peptide Science, 2000; 1(1):
105–124.
Pseudomonas aeruginosa strain 385 produced chitinase antigen. [13] Orinda E, Puspita I D, Putra M P, Ustadi U, Lelana, I Y B. Chitinolytic
enzyme activity of isolate SDI23 from petis and the activity of its partially
4 Conclusions purified enzyme in different pH and temperature (Aktivitas enzim
pendegradasi kitin dari isolat SDI23 asal petis serta karakterisasi ph dan
This study concludes chitinolytic bacteria isolated from blue
suhu dan aktivitas enzim hasil purivikasi parsial. Jurnal Perikanan). J. Fish.
swimmer crab’s cell (Portunus pelagicus) genus of Pseudomonas. Sci, 2015; 17(2): 96–102. (in Indonesian)
The highest chitinase activity was obtained from the supernatant [14] Zhu M M, He H J, Fan M T, Ma H J, Ren H W, Zeng J, et al. Application
culture in the 24th hour, in which enzyme activity value was and optimization of solid-state fermentation process for enhancing
0.149 U/mL as a good potential to degradable chitin ability. polygalacturonase production by Penicillium expansum. Int J Agri & Biol
Eng, 2018; 11(6): 187–194.
[15] Setia I N, Suharjono. Chitinolytic assay and identification of bacteria
Acknowledgements Isolated from shrimp waste based on 16S rDNA sequences. Advances in
The authors would like to thank Fish Quarantine Station Microbiology, 2015; 5: 541–548.
[16] Hemraj V, Dikhsa S, Afneet G. A review commonly used biochemical test
Laboratory Quality Control and Fisheries Product Security Class I
for bacteria. Journal of Life Science, 2013; 1(1): 1–7.
Gorontalo Province of Indonesia, and Pharmaceutical Laboratory [17] Amano M M T, Enokimoto M, Yano T, Moe K K, Misawa N. Influence of
of Universitas Negeri Gorontalo support facility for this research. pH of TSI medium on the detection of hydrogen sulfide production by
campylobacter hyointestinalis. Journal Compilation, 2007; 44: 544–549.
[18] Cowan S C, Steel S. Manual for the identification of medical bacteria.
[References] Cambridge University Press Cambridge, London, 2003.
[1] Bhattacharya D, Nagpure A, Gupta K R. Bacterial chitinases: Properties [19] Wang S L, Chang W T. Purification and characterization of two
and potential. Critical Reviews in Biotechnology, 2008; 27(1): 21–28. bifunctional chitinases/lysozymes extracellularly produced by
[2] Younes I, Bellaaj O G, Nasri R, Chaabouni M, Rinaudo M, Nasri M. Chitin Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium.
and chitosan preparation from shrimp shells using optimized enzymatic Applied and Environmental Microbiology, 1997: 63(2): 380–386.
deproteinization. Journal Process Chemistry, 2012; 47: 2032–2039. [20] Thomson S E, Smith M, Wilkinson M C, Peek K. Identification and
[3] Arbia W, Arbia L, Adour L, Amrane A. Chitin extraction from characterization of chitinase antigen from Pseudomonas aeruginosa strain
crustaceanshells using biological methods. A Review Food Technol 385. Applied and Environmental Microbiology, 2001; 67(9): 4001–4008.