Purification and Properties of a Collagenolytic Protease Produced by Marine Bacterium Vibrio vulnificus CYK279H

Purification and Properties of a Collagenolytic Protease Produced by Marine Bacterium Vibrio vulnificus CYK279H

A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was esti...

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Veröffentlicht in:Biotechnology and bioprocess engineering 2005-11, Vol.10 (6)
Hauptverfasser: Kang, S.I. (Pukyong National University, Busan, Republic of Korea), Jang, Y.B. (Pukyong National University, Busan, Republic of Korea), Choi, Y.J. (Gyeongsang National University, Jinju, Republic of Korea), Kong, J.Y. (Pukyong National University, Busan, Republic of Korea), E-mail: kongjy@pknu.ac.kr
Format: Artikel
Sprache:eng
Schlagworte:
GELATIN
GELATINA
GELATINE
metalloprotease
PROTEASAS
PROTEASE
PROTEASES
PURIFICACION
PURIFICATION
VIBRIO VULNIFICUS
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Zusammenfassung:A collagenolytic enzyme, produced by Vibrio vulnificus CYK279H, was purified by ultrafiltration, dialysis, Q-Sepharose ion exchange and Superdex-200 gel chromatography. The enzyme from the supernatant was purified 13.2 fold, with a yield of 11.4%. The molecular weight of the purified enzyme was estimated by SDS-PAGE to be approximately 35.0 kDa. The N-terminal sequence of the enzyme was determined as Gly-Asp-Pro-Cys-Met-Pro-Ile-Ile-Ser-Asn. The optimum temperature and pH for the enzyme activity were 35℃ and 7.5, respectively.
ISSN:1226-8372
1976-3816
DOI:10.1007/BF02932300