Extracellular alkaline proteases from alkalophilic Vibrio metschnikovii strain RH530

Yong Tae Kwon, Jin Oh Kim, Sun Young Moon, Hyune Hwan Lee, Hyune Mo Rho

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47 Scopus citations


Alkaline proteases, named VapT and VapK, from Gram-negative alkalophilic Vibrio metschnikovii strain RH530 were purified and characterized. Both enzymes had optimum pH and temperature of 10. 5 and 60 °C, respectively. VapT and VapK retained 40 % and 80 %, respectively, of their initial activities at pH 12 after 24-h incubation at 25 °C. The half-lives of VapT and VapK were 10 min and 24 min, respectively, at pH 8 and 60 °C. Addition of Ca2+ extended their half-lives more than 20 fold. VapT and VapK retained over 30 % and 90 %, respectively, of their activities in the presence of 5 % SDS and 8 M urea. Analysis of amino acid composition showed that VapT contained seven cysteine residues and VapK did two. The N-terminal amino acid sequences of the proteases were determined and compared with those of Bacillus licheniformis subtilisin Carlsberg, Vibrio alginolyticus exoprotease A, and Tritirachium album proteinase K.

Original languageEnglish (US)
Pages (from-to)413-418
Number of pages6
JournalBiotechnology Letters
Issue number4
StatePublished - Apr 1994
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology
  • Bioengineering
  • Biotechnology


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