Biocatalysis with the milk protein -lactoglobulin: promoting retroaldol cleavage of ,-unsaturated aldehydes.
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Enzymes with a hydrophobic binding site and an active site lysine have been suggested to be promiscuous in their catalytic activity. -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 ,-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.
author list (cited authors)
Gowda, V., Foley, B., Du, J., Esteb, M., & Watanabe, C.