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
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
تکنولوژی و شیمی فرآیندی
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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
Journal: Bioresource Technology - Volume 99, Issue 17, November 2008, Pages 8088–8094
نویسندگان
Snehasish Basu, Abhrajyoti Ghosh, Amit Bera, Manabendra N. Saha, Dhrubajyoti Chattopadhyay, Krishanu Chakrabarti,