Characterization and Kinetics of 45 kDa Chitosanase fromBacillussp. P16
| العنوان: | Characterization and Kinetics of 45 kDa Chitosanase fromBacillussp. P16 |
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| المؤلفون: | Yong-Woong Kim, Jae-Han Shim, You-Young Jo, Yu-Lan Jin, Ro-Dong Park, Kyu-Jong Jo, Kil-Yong Kim |
| المصدر: | Bioscience, Biotechnology, and Biochemistry. 67:1875-1882 |
| بيانات النشر: | Informa UK Limited, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | Glycoside Hydrolases, Starch, Oligosaccharides, Bacillus, Chitin, Polysaccharide, Applied Microbiology and Biotechnology, Biochemistry, Analytical Chemistry, Chitosan, Hydrolysis, chemistry.chemical_compound, Polysaccharides, Enzyme Stability, Chitosanase, Cellulose, Molecular Biology, chemistry.chemical_classification, Chromatography, biology, Viscosity, Organic Chemistry, Temperature, Acetylation, General Medicine, Hydrogen-Ion Concentration, Enzyme assay, Molecular Weight, carbohydrates (lipids), Kinetics, chemistry, Solvents, biology.protein, Electrophoresis, Polyacrylamide Gel, Salts, Chromatography, Thin Layer, Biotechnology |
| الوصف: | An extracellular 45 kDa endochitosanase was purified and characterized from the culture supernatant of Bacillus sp. P16. The purified enzyme showed an optimum pH of 5.5 and optimum temperature of 60 degrees C, and was stable between pH 4.5-10.0 and under 50 degrees C. The Km and Vmax were measured with a chitosan of a D.A. of 20.2% as 0.52 mg/ml and 7.71 x 10(-6) mol/sec/mg protein, respectively. The enzyme did not degrade chitin, cellulose, or starch. The chitosanase digested partially N-acetylated chitosans, with maximum activity for 15-30% and lesser activity for 0-15% acetylated chitosan. The chitosanase rapidly reduced the viscosity of chitosan solutions at a very early stage of reaction, suggesting the endotype of cleavage in polymeric chitosan chains. The chitosanase hydrolyzed (GlcN)7 in an endo-splitting manner producing a mixture of (GlcN)(2-5). Time course studies showed a decrease in the rate of substrate degradation from (GlcN)7 to (GlcN)6 to (GlcN)5, as indicated by the apparent first order rate constants, k1 values, of 4.98 x 10(-4), 2.3 x 10(-4), and 9.3 x 10(-6) sec(-1), respectively. The enzyme hardly catalyzed degradation of chitooligomers smaller than the pentamer. |
| تدمد: | 1347-6947 0916-8451 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61ac475403422db094a2c149fcd6c2cd https://doi.org/10.1271/bbb.67.1875 |
| رقم الأكسشن: | edsair.doi.dedup.....61ac475403422db094a2c149fcd6c2cd |
| قاعدة البيانات: | OpenAIRE |
PDF full text from Publisher | تدمد: | 13476947 09168451 |
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