Article ID Journal Published Year Pages File Type
49724 Catalysis Communications 2015 5 Pages PDF
Abstract

•ST0779 identified as novel promising promiscuous biocatalyst for aldol addition•Turnover number kcat of ST0779 at 55 °C is 7.78-fold higher than that of PPL at 37 °C.•The catalytic efficiency kcat/Km of ST0779 adds up to 140 times higher than PPL.•Demonstrated the potential to discover novel promiscuous enzymes from the thermophiles

This work, for the first time, demonstrated the catalytic promiscuity of an acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) for aldol addition reaction, which shows accelerated activity at elevated temperature. The turnover number kcat (s− 1) of this thermostable enzyme at 55 °C is 7.78-fold higher than that of porcine pancreatic lipase (PPL) at its optimum temperature of 37 °C, which is one of the best reported enzymes for promiscuous catalysis of aldol reaction; and the molecular catalytic efficiency kcat/Km (M− 1 s− 1) adds up to 140 times higher than PPL.

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Physical Sciences and Engineering Chemical Engineering Catalysis
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