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- Title
Engineering of isoamylase: improvement of protein stability and catalytic efficiency through semi-rational design.
- Authors
Li, Youran; Zhang, Liang; Ding, Zhongyang; Gu, Zhenghua; Shi, Guiyang
- Abstract
Isoamylase catalyzes the hydrolysis of α-1,6-glycosidic linkages in glycogen, amylopectin and α/β-limit dextrins. A semi-rational design strategy was performed to improve catalytic properties of isoamylase from Bacillus lentus. Three residues in vicinity of the essential residues, Arg505, Asn513, and Gly608, were chosen as the mutation sites and were substituted by Ala, Pro, Glu, and Lys, respectively. Thermal stability of the mutant R505P and acidic stability of the mutant R505E were enhanced. The k /K values of the mutant G608V have been promoted by 49 %, and the specific activity increased by 33 %. This work provides an effective strategy for improving the catalytic activity and stability of isoamylase, and the results obtained here may be useful for the improvement of catalytic properties of other α/β barrel enzymes.
- Subjects
AMYLASES; PROTEIN stability; CATALYTIC activity; HYDROLYSIS; BACILLUS (Bacteria)
- Publication
Journal of Industrial Microbiology & Biotechnology, 2016, Vol 43, Issue 1, p3
- ISSN
1367-5435
- Publication type
Article
- DOI
10.1007/s10295-015-1708-4