ArticleJournal of industrial microbiology & biotechnology2016
Engineering of isoamylase: improvement of protein stability and catalytic efficiency through semi-rational design.
Article in Journal of industrial microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 21 citations in OpenAlex.
- Semi-rational engineering of an α-L-fucosidase for regioselective synthesis of fucosyl-Food chemistry. Molecular sciences · 2025Article
- Bacterial amylases enable glycogen degradation by the vaginal microbiome.Nature microbiology · 2023Article
- Protein Stability: Enhancement and Measurement.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Simultaneously improving the specific activity and thermostability of α-amylase BLA by rational design.Bioprocess and biosystems engineering · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
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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.
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