[Procedure for obtaining and catalytic properties of trypsin immobilized in cryogels of polyvinyl alcohol].
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.
Lysogorskaia
E N
EN
Rosliakova
T V
TV
Beliaeva
A V
AV
Bacheva
A V
AV
Lozinskiĭ
V I
VI
Filippova
I Iu
IIu
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*
D004800:Enzymes, Immobilized; D005782:Gels; D009842:Oligopeptides; D011142:Polyvinyl Alcohol; D014357:Trypsin