Versatile de Novo Enzyme Activity in Capsid Proteins from an Engineered M13 Bacteriophage Library

TitleVersatile de Novo Enzyme Activity in Capsid Proteins from an Engineered M13 Bacteriophage Library
Publication TypeJournal Article
Year of Publication2014
AuthorsCasey, JP, Barbero, RJ, Heldman, N, Belcher, AM
JournalJournal of the American Chemical Society
Volume136
Issue47
Pagination16508 - 16514
Date Published2014/11/26/
Abstract

Biocatalysis has grown rapidly in recent decades as a solution to the evolving demands of industrial chemical processes. Mounting environmental pressures and shifting supply chains underscore the need for novel chemical activities, while rapid biotechnological progress has greatly increased the utility of enzymatic methods. Enzymes, though capable of high catalytic efficiency and remarkable reaction selectivity, still suffer from relative instability, high costs of scaling, and functional inflexibility. Herein, we developed a biochemical platform for engineering de novo semisynthetic enzymes, functionally modular and widely stable, based on the M13 bacteriophage. The hydrolytic bacteriophage described in this paper catalyzes a range of carboxylic esters, is active from 25 to 80 degrees C, and demonstrates greater efficiency in DMSO than in water. The platform complements biocatalysts with characteristics of heterogeneous catalysis, yielding high-surface area, thermostable biochemical structures readily adaptable to reactions in myriad solvents. As the viral structure ensures semisynthetic enzymes remain linked to the genetic sequences responsible for catalysis, future work will tailor the biocatalysts to high-demand synthetic processes by evolving new activities, utilizing high-throughput screening technology and harnessing M13s multifunctionality.