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Peptide condensation activity of a neutral protease from Vibrio sp. T1800 (Vimelysin)
Author(s) -
Kunugi Shigeru,
Koyasu Akira,
Takahashi Saori,
Oda Kohei
Publication year - 1997
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19970220)53:4<387::aid-bit5>3.0.co;2-j
Subject(s) - thermolysin , yield (engineering) , protease , neutral protease , chemistry , ethanol , condensation , solvent , peptide , catalysis , enzyme , stereochemistry , biochemistry , physics , thermodynamics , trypsin
Condensation of Cbz‐Asp and PheOMe catalyzed by a neutral protease from Vibrio sp. T1800 (Vimelysin: VLN) was studied. VLN showed a relatively higher catalytic activity of condensation and an apparently larger yield after 3 h or 24 h, in comparison with thermolysin (TLN), especially at lower pH and temperatures. VLN showed higher solvent‐tolerance than TLN. TLhe apparent highest yield (25%) was obtained in 30% DMSO by using VLN; under similar conditions, TLN gave only about a half of this value. The rate of the condensation reaction per mole of enzyme ( v /[ E ] o ) in DMSO 50% at 37°C and pH 6.5 was 0.16 s −1 for VLN and 0.047 s −1 for TLN. In 30% ethanol VLN showed more than three‐fold peptide yield than TLN after 5 h reaction. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 387–390, 1997.