Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports
•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...
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Published in | Enzyme and microbial technology Vol. 60; pp. 47 - 55 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
10.06.2014
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Subjects | |
Online Access | Get full text |
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Summary: | •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 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
ISSN: | 0141-0229 1879-0909 |
DOI: | 10.1016/j.enzmictec.2014.03.013 |