Journal
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
Volume 43, Issue 1, Pages 3-12Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s10295-015-1708-4
Keywords
Isoamylase; Bacillus lentus; Semi-rational design; Structure model; Catalytic efficiency
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Funding
- National Natural Foundation of China [31401674]
- National High-Tech Research and Development Program of China (863 Program) [2011AA100905, 2012AA02120101]
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Isoamylase catalyzes the hydrolysis of alpha-1,6-glycosidic linkages in glycogen, amylopectin and alpha/beta-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 (cat) /K (m) 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 alpha/beta barrel enzymes.
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