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

Autor: K. Peter Stahmann, Andreas Funke, Andrea Merseburg, Klaus Schnitzlein, Susann Barig
Rok vydání: 2014
Předmět:
Polyester resin
genetics [Lipase]
metabolism [Recombinant Proteins]
chemistry [Recombinant Proteins]
metabolism [Lipase]
Applied Microbiology and Biotechnology
Biochemistry
genetics [Glycine Hydroxymethyltransferase]
Substrate Specificity
Organic chemistry
Glycine Hydroxymethyltransferase
chemistry.chemical_classification
chemistry [Glycine Hydroxymethyltransferase]
biology
metabolism [Enzymes
Immobilized]
chemistry [Enzymes
Immobilized]
genetics [Saccharomycetales]
enzymology [Ascomycota]
Recombinant Proteins
genetics [Recombinant Proteins]
Polyester
Resins
Synthetic
visual_art
genetics [Fungal Proteins]
visual_art.visual_art_medium
metabolism [Glycine Hydroxymethyltransferase]
chemistry [Lipase]
Biotechnology
Homotetramer
Polyesters
enzymology [Saccharomycetales]
Bioengineering
Fungal Proteins
Threonine aldolase
genetics [Ascomycota]
chemistry [Fungal Proteins]
Ascomycota
genetics [Enzymes
Immobilized]
ddc:610
Lipase
Protein Structure
Quaternary
Chromatography
Molecular mass
Epoxy Resins
Epoxy
metabolism [Fungal Proteins]
Enzymes
Immobilized
Molecular Weight
Freeze Drying
chemistry
Polymerization
Saccharomycetales
Biocatalysis
biology.protein
Adsorption
Zdroj: Enzyme and microbial technology 60, 47-55 (2014). doi:10.1016/j.enzmictec.2014.03.013
ISSN: 0141-0229
DOI: 10.1016/j.enzmictec.2014.03.013
Popis: 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.
Databáze: OpenAIRE
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