ArticleBMC biotechnology2025
Comparison of active site mutations at subsite + 2 of Anoxybacillus ayderensis A9 β-glucosidase for hydrolysis of pNPG and polydatin.
Article in BMC biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Optimization of Polydatin Hydrolysis Process Through Response Surface Methodology for Efficient Resveratrol Production.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Precision prebiotics: Engineering food-derived polysaccharides to target specific SCFA-producing taxa for neuroprotection via the microbiota-gut-brain axis.Current research in food science · 2026Review
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9 authors.
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Abstract
β-glucosidase from Anoxybacillus ayderensis A9 (BglA9) is a potent enzyme for enzymatic hydrolysis of polydatin to resveratrol. Based on structural and bioinformatics analysis an area near + 2 subsite of the active site pocket of BglA9 was selected and single point mutations were introduced with the aim to enhance the catalytic efficiency of the enzyme towards pNPG and polydatin. The active site region selected for mutations is non-conserved between different glycoside hydrolase family 1 (GH1) enzymes and is located at the end of β-strand 6. The changes introduced in the active site residues were L221S, N222S and G226Q. The E. coli BL21 (DE3) cells were used for the expression of mutant proteins and purification was achieved by Ni-NTA column chromatography. The thermal and pH stability was retained in all the mutants. The proteins with mutated residue resulted in variations in K
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