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Acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) as a novel promiscuous biocatalyst for aldol addition

Paper ID Volume ID Publish Year Pages File Format Full-Text
49724 46763 2015 5 PDF Available
Title
Acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) as a novel promiscuous biocatalyst for aldol addition
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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Keywords
Aldol reaction; Sulfolobus tokodaii peptidase (ST0779); Hydrolase; Catalytic promiscuity; Biocatalysis
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Acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) as a novel promiscuous biocatalyst for aldol addition
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Publisher
Database: Elsevier - ScienceDirect
Journal: Catalysis Communications - Volume 66, 5 June 2015, Pages 111–115
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us