Biocatalysis has emerged as an important technology for meeting the demand for green and sustainable synthesis of various fine chemicals. However, a lack of long-term operational stability coupled with difficulty in recovering and re-using soluble enzymes has often limited their industrial applications. Enzyme immobilization has been shown to enhance their stability under both storage and operational conditions as well as minimizing denaturation. Among the various immobilization strategies, cross-linked enzyme aggregates (CLEAs) technology offers simplicity and rapid optimization and have found wide applications in immobilizing various enzymes.<br/>In terms of synthetic capability and industrial applications, cytochrome P450 enzymes are of particular interest, as they are capable of performing a variety of selective oxifunctionalization on unactivated C-H bonds. Our laboratory has developed light-driven P450 biocatalysts featuring a Ru(II)-diimine photosensitizer covalently attached to P450 heme domain mutants.<br/>We have recently been interested in developing cross-linked P450 aggregates. After screening various linkers, Ru(II)-diimine photosensitizers bearing aldehyde functionality provide P450-CLEAs displaying increase activity compared to their counterpart in solution. We will present our investigation on the various cross-linkers as well as immobilized activity results and optimization of the reaction conditions.

Ru(II)-diimine complexes for cross-linking P450 enzyme aggregates

255th National Meeting (2018)

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