Chitinase activity potential and identification of chitinolytic bacteria isolated of swimmer crab’s cell

Rieny Sulistijowati, . Sudin, Rita Marsuci Harmain

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.

Keywords


biodegradable, chitinase, spectrophotometer, Portunus pelagicus, Pseudomonas

Full Text:

PDF

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

Biotechnol, 2013; 51(1): 12–25.

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.




Copyright (c) 2021 International Journal of Agricultural and Biological Engineering

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

2023-2026 Copyright IJABE Editing and Publishing Office