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• W1985364192 startingPage "629" @default.
• W1985364192 abstract "Three design strategies, based on rational and semi-rational approaches, were employed to investigate the functional impact of thermostability-related amino acid substitutions in the β-glycosidase BglY from Thermus thermophilus. Five beneficial mutations were identified, of which 1 mutation was located in the active cavity of the enzyme and contributed to the released substrate inhibition. Combining all 5 beneficial substitutions resulted in the mutant HF5 with a 4.7-fold increase in half-life, with thermal inactivation at 93 °C, and complete lack of substrate inhibition toward the substrate p-nitrophenyl-β-d-glucopyranoside at lower reaction temperatures. The results of this study provide valuable information on amino acid substitutions related to thermostability and substrate inhibition of BglY." @default.
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• W1985364192 date "2013-02-01" @default.
• W1985364192 modified "2023-10-11" @default.
• W1985364192 title "Design of mutants for enhanced thermostability of β-glycosidase BglY from Thermus thermophilus" @default.
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• W1985364192 doi "https://doi.org/10.1016/j.biortech.2012.12.098" @default.
• W1985364192 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23317553" @default.
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