کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4406650 1618698 2011 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Keratinolytic activity of purified alkaline keratinase produced by Scopulariopsis brevicaulis (Sacc.) and its amino acids profile
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم محیط زیست بوم شناسی
پیش نمایش صفحه اول مقاله
Keratinolytic activity of purified alkaline keratinase produced by Scopulariopsis brevicaulis (Sacc.) and its amino acids profile
چکیده انگلیسی

Sodium dodecyl sulfate–polyacrlyamide gel electrophoresis (SDS–PAGE) was used to assess the purity and molecular weight of the previously purified alkaline keratinase enzyme of Scopulariopsis brevicaulis. The enzyme was homogenous, as seen by a single band of protein, and had an apparent molecular weight of 28.5 kDa. Amino acid profile of the purified keratinase revealed that it was composed of 14 different amino acids with high proportions of glutamic acid (20.86%), alanine (14.52%), glycine (14.21%), leucine (8.59%) and serine (7.81%). The enzyme contained moderate amounts of valine (6.01%), threonine (5.58%) and phenyl alanine (5.22%). The purified enzyme of S. brevicaulis exerted a potent keratinolytic activity and was capable to hydrolyze different keratinaceous materials with highest activity on chicken feathers followed by human nails and human hair.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Saudi Journal of Biological Sciences - Volume 18, Issue 2, April 2011, Pages 117–121
نویسندگان
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