Generation of a Highly Stable Reusable Biocatalyst by Entrapment of an Oligomeric Enzyme in Ultra-Large-Pore Mesoporous Silica

Abstract

Phenylalanine ammonia lyase (PAL, E.C.4.3.1.24), was entrapped in ultra-large-pore mesoporous silica (ULPS, 23 nm pore diameter) generating a recyclable, separable biocatalyst. The entrapped ULPS-PAL materials showed excellent stabilization, even after significant exposure to prolonged heating. Additionally, the entrapped ULPS-PAL materials showed extremely high catalytic activity in the deamination of L-phenylalanine to trans-cinnamic acid in aqueous solution and were recovered and recycled up to five times without any observable loss in activity. This approach is simple and capitalizes on the facile synthesis and easy recoverability of mesoporous silicas to generate a stable, reusable PAL-based biocatalyst.

Richard (Rick) Francis Langler Memorial Issue

“…[10] Rick's former undergraduate research student, Stephanie MacQuarrie (Cape Breton University) and colleagues, including three undergraduate research students, report on the stabilisation and improved catalysis of the enzyme phenylalanine ammonium lyase. [11] Diane A. Dickie (University of New Mexico), another former student inspired by Rick's teaching and high standards, along with her colleagues describe their synthesis and characterisation of zwitterionic CS2 adducts of bis(dialkylphosphino) amines. [12] Catalytic asymmetric C-C formation implementing terminal alkyl-metal nucleophiles in tandem hydrometallationisomerisation is reported by Stephen Fletcher and his research students from the University of Oxford.…”