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• W4312095220 abstract "Abstract Esterases are among the most studied enzymes, and their applications expand into several branches of industrial biotechnology. Yet, despite the fact that information on their substrate specificity is crucial for selecting or designing the best fitted biocatalyst for the desired application, it cannot be predicted from their amino acid sequence. In this work, we studied the substrate scope of the newly discovered hydrolytic extremozyme, EstDZ3, against a library of esters with variable carbon chain lengths in an effort to understand the crucial amino acids for the substrate selectivity of this enzyme. EstDZ3 appears to be active against a wide range of esters with high selectivity towards medium‐ to long‐carbon chain vinyl esters. In‐silico studies of its 3D structure revealed that the selectivity might arise from the mainly hydrophobic nature of the active site's environment." @default.
• W4312095220 created "2023-01-04" @default.
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• W4312095220 date "2023-01-31" @default.
• W4312095220 modified "2023-10-17" @default.
• W4312095220 title "Substrate Specificity of the Highly Thermostable Esterase EstDZ3" @default.
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• W4312095220 doi "https://doi.org/10.1002/cbic.202200642" @default.
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