ArticleWorld journal of microbiology & biotechnology2015
Characterization of an extracellular thermophilic chitinase from Paenibacillus thermoaerophilus strain TC22-2b isolated from compost.
Article in World journal of microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Bacterial chitinases: genetics, engineering and applications.World journal of microbiology & biotechnology · 2022Review
- Genomic attributes of thermophilic and hyperthermophilic bacteria and archaea.World journal of microbiology & biotechnology · 2022Review
- Bioconversion of chitin waste through Stenotrophomonas maltophilia for production of chitin derivatives as a Seabass enrichment diet.Scientific reports · 2022Article
- Biochemical purification and characterization of a truncated acidic, thermostable chitinase from marine fungus for N-acetylglucosamine production.Frontiers in bioengineering and biotechnology · 2022Article
- Production of Thermophilic Chitinase byPolymers · 2021Article
- The Draft Genome Sequence and Analysis of an Efficiently Chitinolytic Bacterium Chitinibacter sp. Strain GC72.Current microbiology · 2020Article
- Bioprocessing of Squid Pens Waste into Chitosanase byPolymers · 2020Article
- Article
- Production of a Thermostable Chitosanase from Shrimp Heads viaMarine drugs · 2019Article
- Reclamation of Marine Chitinous Materials for Chitosanase Production via Microbial Conversion byMarine drugs · 2018Article
- Molecular characterization of a novel chitinaseBiotechnology for biofuels · 2018Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paenibacillus thermoaerophilus strain TC22-2b, a thermophilic bacterium with an optimum growth temperature of 50-55 °C isolated from compost (55 °C) in Japan, secreted a chitinase into culture medium in the presence of colloidal chitin. Adding glucose, lactose, mannose, or sucrose to culture medium decreased the amount of chitinase in culture supernatants. This chitinase was purified by ammonium sulfate precipitation, colloidal chitin adsorption, and ion exchange chromatography. The apparent molecular mass of this enzyme was approximately 48 kDa, and its N-terminal amino acid sequence was determined to be Ala-Val-Ser-Thr-Gly-Lys-Lys. The optimum temperature and pH for chitinase activity were 60 °C and pH 4, respectively. The chitinase retained 68 % of its initial activity after incubation at 50 °C for 2 h. Using p-nitrophenyl N,N'-diacetyl-β-D-chitobioside [pNP-(GlcNAc)2] as a substrate, the K m, V max, and k cat values for this enzyme were 1.4 mM, 0.058 mM min(-1), and 9.6 s(-1), respectively. Analysis of hydrolysis products showed that the chitinase digested N-acetyl-chitooligosaccharides in an endo manner. N-acetylglucosamine dimers were not degraded by the enzyme. When colloidal chitin was used as the substrate, N-acetylglucosamine dimers, -trimers, and -tetramers were detected as hydrolysis products. Thus, the thermophilic chitinase may prove useful for industrial applications in chitooligosaccharide production from chitin biomass.
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