کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1189527 963513 2007 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus
چکیده انگلیسی

Transglutaminase (TGase, EC 2.3.2.13) from a Streptomyces hygroscopicus strain isolated from soil was purified from culture broth by ethanol precipitation, followed by successive chromatographies on CM-cellulose and Sephadex G-75 columns with a yield and purification-fold of 21.1% and 30%, respectively. The enzyme’s molecular weight was estimated as 38,000 Da by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified microbial transglutaminase (MTG) exhibited optimum activity at 37–45 °C and in a range of pH 6.0–7.0 for hydroxamate formation from N-carboxybenzoyl-l-glutaminyl-glycine and hydroxylamine. The enzyme was not stable above 50 °C and was stable within a pH range of 5.0–8.0 at lower temperature. The MTG was not inhibited by Ca2+ and ethylenediaminetetraacetic acid, suggesting it was calcium-independent. Purified MTG was strongly inactivated by 5,5′-dithiobis (2-nitrobenzoic acid), Cu2+, Zn2+, Pb2+, and Hg2+, suggesting that this enzyme could possess a thiol group at the active site. The MTG stability was strongly affected by ethanol concentration. The enzyme activity was slightly elevated at a lower concentration of ethanol at 25 °C.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 105, Issue 2, 2007, Pages 612–618
نویسندگان
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