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Promiscuous protease-catalyzed aldol reactions: A facile biocatalytic protocol for carbon–carbon bond formation in aqueous media

Paper ID Volume ID Publish Year Pages File Format Full-Text
24140 43500 2010 7 PDF Available
Title
Promiscuous protease-catalyzed aldol reactions: A facile biocatalytic protocol for carbon–carbon bond formation in aqueous media
Abstract

Several proteases, especially pepsin, were observed to directly catalyze asymmetric aldol reactions. Pepsin, which displays well-documented proteolytic activity under acidic conditions, exhibited distinct catalytic activity in a crossed aldol reaction between acetone and 4-nitrobenzaldehyde with high yield and moderate enantioselectivity. Fluorescence experiments indicated that under neutral pH conditions, pepsin maintains its native conformation and that the natural structure plays an important role in biocatalytic promiscuity. Moreover, no significant loss of enantioselectivity was found even after four cycles of catalyst recycling, showing the high stability of pepsin under the selected aqueous reaction conditions. This case of biocatalytic promiscuity not only expands the application of proteases to new chemical transformations, but also could be developed into a potentially valuable method for green organic synthesis.

Keywords
Biocatalytic promiscuity; Protease; Pepsin; Aldol reaction
First Page Preview
Promiscuous protease-catalyzed aldol reactions: A facile biocatalytic protocol for carbon–carbon bond formation in aqueous media
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 150, Issue 4, December 2010, Pages 539–545
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering