Abstract
Effect of various organic co-solvents on catalytic activity and structural stability of three different Bacillus enzymes, including Bacillus licheniformis γ-glutamyltranspeptidase (BlGGT) and aldehyde dehydrogenase (BlALDH), and Bacillus stearothermophilus aminopeptidase II (BsAPII) were investigated. The experimental results revealed that almost all co-solvents had a detrimental effect on catalytic activity and molecular structure of enzymes at high concentrations. Acetonitrile and dimethylformamide caused a highest degree of enzyme inactivation; however, other more hydrophilic co-solvents, such as ethylene glycol and dimethyl sulfoxide, were better tolerated. High residual activity of BlGGT was obtained in the majority of organic co-solvents tested, but catalytic activities of BlALDH and BsAPII were significantly decreased by the respective concentrations of the same co-solvents. Collectively, the favorable influence of these co-solvents on both catalytic activity and structural stability of BlGGT makes this enzyme more suitable for biocatalytic applications.
Published Version
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