Literature DB >> 24835099

Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports.

Susann Barig1, Andreas Funke2, Andrea Merseburg2, Klaus Schnitzlein3, K-Peter Stahmann2.   

Abstract

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 34kDa, while A. gossypii threonine aldolase expressed in Escherichia coli is a pyridoxal-5'-phosphate binding homotetramer with a mass of 180kDa. 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.
Copyright © 2014 Elsevier Inc. All rights reserved.

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Keywords:  Ashbya gossypii threonine aldolase; Cross linked enzyme aggregates; Epoxy resin; Immobilization; Polyester resin; Thermomyces lanuginosus lipase

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Year:  2014        PMID: 24835099     DOI: 10.1016/j.enzmictec.2014.03.013

Source DB:  PubMed          Journal:  Enzyme Microb Technol        ISSN: 0141-0229            Impact factor:   3.493


  1 in total

Review 1.  Threonine aldolases: perspectives in engineering and screening the enzymes with enhanced substrate and stereo specificities.

Authors:  Kateryna Fesko
Journal:  Appl Microbiol Biotechnol       Date:  2016-01-26       Impact factor: 4.813

  1 in total

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