Dry entrapment of enzymes by epoxy or polyester resins hardened on different solid supports.
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.
Brandenburg University of Technology Cottbus - Senftenberg, Fakultät 6, Großenhainer Str. 57, D-01958 Senftenberg, Germany. Electronic address: susann.barig@hs-lausitz.de.
Susann
S
Barig
Brandenburg University of Technology Cottbus - Senftenberg, Fakultät 6, Großenhainer Str. 57, D-01958 Senftenberg, Germany.
Andreas
A
Funke
Brandenburg University of Technology Cottbus - Senftenberg, Fakultät 6, Großenhainer Str. 57, D-01958 Senftenberg, Germany.
Andrea
A
Merseburg
Brandenburg University of Technology Cottbus - Senftenberg, Fakultät 4, Universitätsplatz 3-4, D-03046 Cottbus, Germany.
Klaus
K
Schnitzlein
Brandenburg University of Technology Cottbus - Senftenberg, Fakultät 6, Großenhainer Str. 57, D-01958 Senftenberg, Germany.
K-Peter
KP
Stahmann
D000327:Adsorption; D001203:Ascomycota / Q000201:enzymology / Q000235:genetics; D055162:Biocatalysis; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004853:Epoxy Resins; D005612:Freeze Drying; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012696:Glycine Hydroxymethyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008970:Molecular Weight; D011091:Polyesters; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012117:Resins, Synthetic; D004718:Saccharomycetales / Q000201:enzymology / Q000235:genetics; D013379:Substrate Specificity
D004800:Enzymes, Immobilized; D004853:Epoxy Resins; D005656:Fungal Proteins; D011091:Polyesters; D011994:Recombinant Proteins; D012117:Resins, Synthetic; D012696:Glycine Hydroxymethyltransferase; D008049:Lipase
Ashbya gossypii threonine aldolase; Cross linked enzyme aggregates; Epoxy resin; Immobilization; Polyester resin; Thermomyces lanuginosus lipase