Generation of a Highly Stable Reusable Biocatalyst by Entrapment of an Oligomeric Enzyme in Ultra-Large-Pore Mesoporous Silica*
Christopher B. J. MacDonald A , Matthew F. Tobin A , Anna E. Morrison A , Mary E. Tait A , Godwin B. D’Cunha A and Stephanie L. MacQuarrie A B
+ Author Affiliations
- Author Affiliations
A Department of Chemistry, Cape Breton University, 1250 Grand Lake Road, Sydney, Nova Scotia, Canada, B1P6L2.
B Corresponding author. Email: Stephanie_MacQuarrie@cbu.ca
Australian Journal of Chemistry 68(3) 396-400 https://doi.org/10.1071/CH14603
Submitted: 4 October 2014 Accepted: 21 November 2014 Published: 23 December 2014
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.
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