کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
18420 42722 2008 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and properties of an acetylxylan esterase from Thermobifida fusca
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Purification and properties of an acetylxylan esterase from Thermobifida fusca
چکیده انگلیسی

An acetylxylan esterase from Thermobifida fusca NTU22 was purified 51-fold as measured by specific activity from crude culture filtrate by ultrafiltration concentration, Sepharose CL-6B and DEAE-Sepharose CL-6B column chromatography. The overall yield of the purified enzyme was 14.4%. The purified enzyme gave an apparent single protein band on an SDS-PAGE. The molecular mass of purified enzyme as estimated by SDS-PAGE and by gel filtration on Sepharose CL-6B was found to be 30 and 28 kDa, respectively, indicating that the acetylxylan esterase from T. fusca NTU22 is a monomer. The pI value of the purified enzyme was estimated to be 6.55 by isoelectric focusing gel electrophoresis. The N-terminal amino acid sequence of the purified esterase was ANPYERGP. The optimum pH and temperature for the purified enzyme were 8.0 and 80 °C, respectively. The Zn2+, Hg2+, PMSF and DIPF inhibited the enzyme activity. The Km value for p-nitrophenyl acetate and acetylxylan were 1.86 μM and 0.15%, respectively. Co-operative enzymatic degradation of oat-spelt xylan by purified acetylxylan esterase and xylanase significantly increased the acetic acid liberation compared to the acetylxylan esterase action alone.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 42, Issue 2, January 2008, Pages 181–186
نویسندگان
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