کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
684534 889023 2008 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی تکنولوژی و شیمی فرآیندی
پیش نمایش صفحه اول مقاله
Thermodynamic characterization of a highly thermoactive extracellular pectate lyase from a new isolate Bacillus pumilus DKS1
چکیده انگلیسی

An extracellular pectate lyase (EC 4.2.2.2) was purified from the culture filtrate of a newly isolated Bacillus pumilus DKS1 grown in pectin containing medium. Using ion-exchange and gel filtration chromatography, this enzyme was purified and found to have a molecular weight of around 35 kDa. The purified enzyme exhibited maximal activity at a temperature of 75 °C and pH 8.5. The presence of 1 mM calcium and manganese enhanced pectate lyase activity and was strongly inhibited by zinc, nickel and EDTA. The thermal inactivation studies revealed an entropy–enthalpy compensation pattern below a critical temperature. The alkaliphilicity and high thermostability of this pectate lyase may have potential implications in fibre degumming.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioresource Technology - Volume 99, Issue 17, November 2008, Pages 8088–8094
نویسندگان
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