title: [Procedure for obtaining and catalytic properties of trypsin immobilized in cryogels of polyvinyl alcohol].
abstract: Commercial preparations of trypsin, varying in activity, were immobilized in a cryogel of polyvinyl alcohol, activated by dialdehydes (terephthalic, succinic, or glutaric) or divinyl sulfone. All preparations of the immobilized enzyme exhibited hydrolytic activity and retained stability for 8 months. In an organic solvent environment, specimens of immobilized trypsin catalyzed the synthesis of N-carbobenzoxy-L-phenylalanyl-L-arginyl-L-leucine p-nitroanilide from N-carbobenzoxy-L-phenylalanyl-L-argininine methyl ester (or N-carbobenzoxy-L-phenylalanyl-L-arginine) and L-leucine p-nitroanilide, as well as the formation of N-carbobenzoxy-L-alanyl-L-alanyl-L-arginyl-L-phenylalanine p-nitroanilide from N-carbobenzoxy-L-alanyl-L-alanyl-L-arginine and L-phenylalanine p-nitroanilide. The presence of small amounts of water in organic solvents was prerequisite to the biocatalysts manifesting synthase activity in reactions of peptide bond formation.
authors.forename: E N
authors.initials: EN
authors.lastname: Lysogorskaia
authors.forename: T V
authors.initials: TV
authors.lastname: Rosliakova
authors.forename: A V
authors.initials: AV
authors.lastname: Beliaeva
authors.forename: A V
authors.initials: AV
authors.lastname: Bacheva
authors.forename: V I
authors.initials: VI
authors.lastname: Lozinskiĭ
authors.forename: I Iu
authors.initials: IIu
authors.lastname: Filippova
mesh_terms: D000818:Animals; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005782:Gels / Q000737:chemistry; D009842:Oligopeptides / Q000138:chemical synthesis*; D011142:Polyvinyl Alcohol / Q000737:chemistry*; D013552:Swine; D014357:Trypsin / Q000737:chemistry*
chemical_list: D004800:Enzymes, Immobilized; D005782:Gels; D009842:Oligopeptides; D011142:Polyvinyl Alcohol; D014357:Trypsin