Biocatalysis with the milk protein β-lactoglobulin: promoting retroaldol cleavage of α,β-unsaturated aldehydes Academic Article uri icon

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.

author list (cited authors)

  • Gowda, V., Foley, B., Du, J., Esteb, M., & Watanabe, C.

citation count

  • 1

publication date

  • January 2018