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

Biotechnology and Bioengineering
S KunugiK Oda

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.

References

Jun 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·S I Wayne, J S Fruton
Sep 1, 1980·Journal of Biochemistry·T Oka, K Morihara
Sep 26, 1995·Biochemistry·P P WangikarJ S Dordick
Oct 15, 1996·European Journal of Biochemistry·S KunugiK Oda
Oct 1, 1996·Bioscience, Biotechnology, and Biochemistry·S TakahashiK Oda
Jan 20, 1992·Biotechnology and Bioengineering·P MartinezF H Arnold

Citations

Feb 28, 2006·Journal of Industrial Microbiology & Biotechnology·J A VázquezM A Murado
Aug 17, 2011·Applied Microbiology and Biotechnology·Ji-Wei Wu, Xiu-Lan Chen

Related Concepts

Ethanol
Calpain
Dimethyl Sulfoxide
Peptides
Thermolysin
N-carbobenzyloxyalanine
Vimelysin
Vibrio species

Related Feeds

Bioinformatics in Biomedicine

Bioinformatics in biomedicine incorporates computer science, biology, chemistry, medicine, mathematics and statistics. Discover the latest research on bioinformatics in biomedicine here.