Article ID Journal Published Year Pages File Type
16934 Enzyme and Microbial Technology 2014 9 Pages PDF
Abstract

•A dry entrapment immobilization method for enzymes was evolved.•Therefore water-free enzyme preparations were embedded in two different polymeric glues.•The method was proofed to be applicable on two very different enzymes, a lipase and a threonine aldolase.

Embedding of enzymes was performed with epoxy or polyester resin by mixing in a dried enzyme preparation before polymerization was started. This fast and low-cost immobilization method produced enzymatically active layers on different solid supports.As model enzymes the well-characterized Thermomyces lanuginosus lipase and a new threonine aldolase from Ashbya gossypii were used. It was shown that T. lanuginosus lipase recombinantly expressed in Aspergillus oryzae is a monomeric enzyme with a molecular mass of 34 kDa, while A. gossypii threonine aldolase expressed in Escherichia coli is a pyridoxal-5′-phosphate binding homotetramer with a mass of 180 kDa.The enzymes were used freeze dried, in four different preparations: freely diffusing, adsorbed on octyl sepharose, as well as cross-linked enzyme aggregates or as suspensions in organic solvent. They were mixed with standard two-component resins and prepared as layers on solid supports made of different materials e.g. metal, glass, polyester. Polymerization led to encapsulated enzyme preparations showing activities comparable to literature values.

Related Topics
Physical Sciences and Engineering Chemical Engineering Bioengineering
Authors
, , , , ,