期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 69, 期 -, 页码 46-51出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2014.05.024
关键词
Bacillus thuringiensis AD-12; Keratinolytic proteinase; Keratin biodegradation
资金
- MITA (Agency of Science, Innovation and Technology) program Development of Industrial Biotechnology in Lithuania
- project Innovative Tools for Cosmetic Industry (COSMETIZYM) [MITA 31V-18]
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据