Peptide condensation activity of a neutral protease from Vibrio sp. T1800 (Vimelysin)

✍ Scribed by Shigeru Kunugi; Akira Koyasu; Saori Takahashi; Kohei Oda

• Book ID: 101242036
• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 99 KB
• Volume: 53
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/(sici)1097-0290(19970220)53:4<387::aid-bit5>3.0.co;2-j

✦ Synopsis

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.