title: Peptide condensation activity of a neutral protease from Vibrio sp. T1800 (Vimelysin).
abstract: 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 degrees 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. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 387-390, 1997.
authors.affiliation: Laboratory for Biopolymer Physics, Department of Polymer Science and Engineering, Kyoto Institute of Technology, Kyoto, 606, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Kunugi
authors.forename: A
authors.initials: A
authors.lastname: Koyasu
authors.forename: S
authors.initials: S
authors.lastname: Takahashi
authors.forename: K
authors.initials: K
authors.lastname: Oda