| Literature DB >> 28191945 |
Somayesadat Badieyan1, Qiuming Wang1, Xingquan Zou1, Yaoxin Li1, Maggie Herron2, Nicholas L Abbott2, Zhan Chen1, E Neil G Marsh1.
Abstract
In the absence of aqueous buffer, most enzymes retain little or no activity; however, "water-free" enzymes would have many diverse applications. Here, we describe the chemically precise immobilization of an enzyme on an engineered surface designed to support catalytic activity in air at ambient humidity. Covalent immobilization of haloalkane dehalogenase on a surface support displaying poly(sorbitol methacrylate) chains resulted in ∼40-fold increase in activity over lyophilized enzyme powders for the gas-phase dehalogenation of 1-bromopropane. The activity of the immobilized enzyme in air approaches 25% of the activity obtained in buffer for the immobilized enzyme. Poly(sorbitol methacrylate) appears to enhance activity by replacing protein-water interactions, thereby preserving the protein structure.Entities:
Year: 2017 PMID: 28191945 DOI: 10.1021/jacs.6b12174
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419