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 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 α/β barrel enzymes.
journal_name
J Ind Microbiol Biotechnoljournal_title
Journal of industrial microbiology & biotechnologyauthors
Li Y,Zhang L,Ding Z,Gu Z,Shi Gdoi
10.1007/s10295-015-1708-4subject
Has Abstractpub_date
2016-01-01 00:00:00pages
3-12issue
1eissn
1367-5435issn
1476-5535pii
10.1007/s10295-015-1708-4journal_volume
43pub_type
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journal_title:Journal of industrial microbiology & biotechnology
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journal_title:Journal of industrial microbiology & biotechnology
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journal_title:Journal of industrial microbiology & biotechnology
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