کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7234839 | 1471012 | 2018 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cloning and characterization of a chitinase from Thermobifida fusca reveals Tfu_0580 as a thermostable and acidic endochitinase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی انرژی
انرژی های تجدید پذیر، توسعه پایدار و محیط زیست
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چکیده انگلیسی
Being capable of hydrolyzing chitin, chitinases have various applications such as production of N-acetylchitooligosaccharides (COSs) and N-acetylglucosamine (GlcNAc), degrading chitin as a consolidated bioprocessing, and bio-control of fungal phytopathogens. Here, a putative chitinase in Thermobifida fusca, Tfu_0580, is characterized. Tfu_0580 was purified by homogeneity with a molecular weight of 44.9â¯kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis. Tfu_0580 displayed a clear activity against colloidal chitin, which is comparable to a commercial Streptomyces griseus chitinase. Enzyme activities against p-nitrophenyl β-D-N,Nâ²,Nâ²â²-triacetylchitotriose (p-NP-(GlcNAc)3), N,Nâ²-diacetyl-β-D-chitobioside (p-NP-(GlcNAc)2) and p-nitrophenyl N-acetyl-β-D-glucosaminide (p-NP-(GlcNAc)) showed that Tfu_0580 exhibited highest activity against p-NP-(GlcNAc)3. Further optimization of the enzyme activity conditions showed: 1) an optimum catalytic activity at pH 6.0 and 30â¯Â°C; 2) activity over broad pH (4.8-7.5) and temperature (20-55â¯Â°C); 3) stimulation of activity by the metallic ions Ca2+ and Mn2+.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biotechnology Reports - Volume 19, September 2018, e00274
Journal: Biotechnology Reports - Volume 19, September 2018, e00274
نویسندگان
Qiang Yan, Stephen S. Fong,