Keratinolytic proteinase from Bacillus thuringiensis AD-12

被引：23

作者：

Gegeckas, Audrius ^{[1
]}

Gudiukaite, Renata ^{[1
]}

Citavicius, Donaldas ^{[1
]}

机构：

[1] Vilnius State Univ, Fac Nat Sci, Dept Microbiol & Biotechnol, LT-03101 Vilnius, Lithuania

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2014年 / 69卷

关键词：

Bacillus thuringiensis AD-12; Keratinolytic proteinase; Keratin biodegradation; KERATINASE; PURIFICATION; IDENTIFICATION; ENZYME; GENE;

D O I：

10.1016/j.ijbiomac.2014.05.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new isolated strain noted to produce a novel detergent-stable serine keratinolytic proteinase and identified as Bacillus thuringiensis AD-12. Native keratinolytic proteinase from B. thuringiensis (BtKER) was purified and characterized. The purified BtKER enzyme is a monomer with a molecular mass of 39 kDa. Biochemical characterization assays revealed that the BtKER attained optimal activity at pH 7 and 30 degrees C. Residual activity after 1 h incubation at 50 degrees C was higher than 80%. The enzyme was activated and stabilized by Mn2+ and Li+ metal ions but inactivated by organic solvents. Purified BtKER showed the highest substrate specificity toward keratin from wool > sodium caseinate > collagen > BSA > gelatin in descending order. BtKER is the first reported keratinolytic proteinase from B. thuringiensis and obtained results suggested that new characterized enzyme can be a powerful biocatalyst in peptide production associated to hydrolysis of keratinous and/or keratin-like waste. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：46 / 51

页数：6

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