Isolation and Characterization of Mucinase Complex Secreted from Vibrio parahaemolyticus

Mucinase complex from V. parahaemolyticus ATCC 17802 was purified 6-fold with 0.4% yield by two sequential steps of Q-Sepharose and Superdex 200HR showed at least 8 times higher mucin-degrading activity than the culture filtrates. The mucinase complex also showed gelatin and casein-hydrolyzing activ...

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Veröffentlicht in:	Journal of microbiology and biotechnology 2003-10, Vol.13 (5), p.731-737
Hauptverfasser:	Jun, I.J, Kim, Y.H, Kim, M.J, Hwang, H.S, Lee, T.H, Cha, J.H. (Pusan National University, Busan, Republic of Korea)
Format:	Artikel
Sprache:	eng
Schlagworte:	Biological and medical sciences Biotechnology Fundamental and applied biological sciences. Psychology mucin
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Zusammenfassung:	Mucinase complex from V. parahaemolyticus ATCC 17802 was purified 6-fold with 0.4% yield by two sequential steps of Q-Sepharose and Superdex 200HR showed at least 8 times higher mucin-degrading activity than the culture filtrates. The mucinase complex also showed gelatin and casein-hydrolyzing activities, which demonstrates that the protein is a complex compound containing several proteases. The optimum pH and temperature of partially purified mucinase complex compound containing several proteases.
ISSN:	1017-7825