Hydrolase-catalysed synthesis of peroxycarboxylic acids: Biocatalytic promiscuity for practical applications.
The enzymatic promiscuity concept involves the possibility that one active site of an enzyme can catalyse several different chemical transformations. A rational understanding of the mechanistic reasons for this catalytic performance could lead to new practical applications. The capability of certain hydrolases to perform the perhydrolysis was described more than a decade ago, and recently its molecular basis has been elucidated. Remarkably, a similarity between perhydrolases (cofactor-free haloperoxidases) and serine hydrolases was found, with both groups of enzymes sharing a common catalytic triad, which suggests an evolution from a common ancestor. On the other hand, several biotechnological applications derived from the capability of hydrolases to catalyse the synthesis of peracids have been reported: the use of hydrolases as bleaching agents via in situ generation of peracids; (self)-epoxidation of unsaturated fatty acids, olefins, or plant oils, via Prileshajev epoxidation; Baeyer-Villiger reactions. In the present review, the molecular basis for this promiscuous hydrolase capability, as well as identified applications are reviewed and described in detail.
Carboni-Oerlemans
Chiara
C
Akzo Nobel Chemicals BV, Chemicals Process Technology Department (CPT), Velperweg 76, PO Box 9300, 6800 SB Arnhem, The Netherlands. Chiara.carboni@akzonobel-chemicals.com
Domínguez de María
Pablo
P
Tuin
Bernard
B
Bargeman
Gerrald
G
van der Meer
Ab
A
van Gemert
Robert
R
D001709:Biotechnology / Q000379:methods* / Q000639:trends; D002264:Carboxylic Acids / Q000737:chemistry*; D002384:Catalysis; D004789:Enzyme Activation; D006867:Hydrolases / Q000737:chemistry*; D013379:Substrate Specificity
D002264:Carboxylic Acids; D006867:Hydrolases