期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 111, 期 -, 页码 917-922出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2018.01.105
关键词
Protease; Entrapment; Agar-agar; Stability; Reutilization efficiency
资金
- Karachi Institute of Biotechnology and Genetic Engineering (KIBGE), University of Karachi, Pakistan
The catalytic performance of an immobilized enzyme could be enhanced by using entrapment technique. In this contemporary study agar-agar, a natural polysaccharide, is subjected to entrap serine-protease produced by Aspergillus niger KIBGE-IB36. The results revealed that maximum enzymatic activity was attained when 3.0% agar agar was used. It was observed that in case of both free and entrapped forms the enzyme was stable at pH-5.0. While, an increment in reaction temperature and time was noticed from 50 to 55 degrees C and 15.0 to 20.0 min, respectively. K-m value increased from 1.883 mM to 2.399 mM and V-max value decreased from 1753 U mg(-1) to 1372 U mg(-1) after agar-agar entrapment of protease as compared to soluble enzyme. Additionally, entrapped protease within the polymer exhibited significant increase in the thermal stability at various temperatures and retained approximately 68.0% of its residual activity at 60 degrees C. However, at this extreme temperature the soluble protease lost its catalytic performance. Storage stability considerably improved as entrapped protease revealed enzymatic activity up to 30 days as compared to soluble enzyme. Recycling efficiency was calculated up to eight cycles which is an exceptional characteristic for economic feasibility and continuous reusability of protease. (C) 2018 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