کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2020543 1069187 2013 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus
چکیده انگلیسی

Keratinolytic proteases find extensive applications both in environmental biotechnology and pharmaceutical industries. An extracellular keratinolytic protease was purified and characterized from the fungus, Aspergillus parasiticus, isolated from poultry soil. The enzyme was purified to homogeneity by acetone and ammonium sulfate precipitations followed by CM-Sepharose column chromatography. The molecular mass of the enzyme was 36 kDa as judged by SDS–PAGE. The purified keratinase had a pH optimum of 7.0 and temperature optimum of 50 oC. The enzyme hydrolyzed the substrate azocasein and the Km and Vmax of the purified keratinase were found to be 1.04 mg/ml and 3463.34 Units/min/mg protein, respectively. The enzyme showed increased activity in the presence of reducing agents. The enzyme was found to be glycosylated. According to the inhibition profiles obtained with the various protease inhibitors, it was confirmed that the purified keratinase belongs to the serine protease type. The purified enzyme activity was enhanced by calcium, magnesium and manganese ions and partially inhibited by cadmium, copper and zinc ions. The purified enzyme showed increased activity with nonionic detergents and urea.


► A keratinase from Aspergillus parasiticus has been purified to homogeneity and characterized.
► The enzyme is found to be glycosylated.
► The enzyme may find potential applications in waste treatment and cosmetic industries.
► Lower Km value and broad pH and temperature optima are useful for applications.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 88, Issue 2, April 2013, Pages 214–220
نویسندگان
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