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Issue 13, 2018
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Biocatalysis with the milk protein β-lactoglobulin: promoting retroaldol cleavage of α,β-unsaturated aldehydes

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Abstract

Enzymes with a hydrophobic binding site and an active site lysine have been suggested to be promiscuous in their catalytic activity. β-Lactoglobulin (BLG), the principle whey protein found in milk, possesses a central calyx that binds non-polar molecules. Here, we report that BLG can catalyze the retro-aldol cleavage of α,β-unsaturated aldehydes making it a naturally occurring protein capable of catalyzing retro-aldol reactions on hydrophobic substrates. Retroaldolase activity was seen to be most effective on substrates with phenyl or naphthyl side-chains. Use of a brominated substrate analogue inhibitor increases the product yield by a factor of three. BLG's catalytic activity and its ready availability make it a prime candidate for the development of commercial biocatalysts.

Graphical abstract: Biocatalysis with the milk protein β-lactoglobulin: promoting retroaldol cleavage of α,β-unsaturated aldehydes

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Publication details

The article was received on 17 Jan 2018, accepted on 26 Feb 2018 and first published on 27 Feb 2018


Article type: Communication
DOI: 10.1039/C8OB00139A
Citation: Org. Biomol. Chem., 2018,16, 2210-2213
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    Biocatalysis with the milk protein β-lactoglobulin: promoting retroaldol cleavage of α,β-unsaturated aldehydes

    V. Gowda, B. Foley, J. Du, M. Esteb and C. M. H. Watanabe, Org. Biomol. Chem., 2018, 16, 2210
    DOI: 10.1039/C8OB00139A

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