Purification and Characterization of the Intracellular Alginase from Vibrio sp. AL-145

알긴산 분해균 Vibrio sp. AL-145가 생산하는 균체내 효소의 정제 및 특성

  • Joo, Dong-Sik ;
  • Lee, Jung-Suk ;
  • Park, Jung-Je ;
  • Cho, Soon-Yeong ;
  • Ahn, Chang-Bum ;
  • Lee, Eung-Ho
  • 주동식 (부산수산대학교 식품공학과) ;
  • 이정석 (부산수산대학교 식품공학과) ;
  • 박중제 (부산수산대학교 식품공학과) ;
  • 조순영 (강릉대학교 식품과학과) ;
  • 안창범 (여수수산대학교 식품영양학과) ;
  • 이응호 (부산수산대학교 식품공학과)
  • Published : 1995.08.01


The intracellular alginase from Vibrio sp. AL-145 was purified by ion chromatography on DEAE-Cellulose column, Q-Sepharose column, and gel filtration on Sephadex G-100 column. The optimum pH and temperature for the activity of the purified intracellular enzyme were 8.0 and 37$\circ$C, respectively. The enzyme was stable at the pH range of 7.5-8.5, and at 30$\circ$C for 30 min. The molecular weight of the intracellular enzyme was estimated to be about 23, 000 daltons by SDS-polyacrylamide gel electrophoresis. NaCl was required for enzyme activity and the optimum concentration was 0.5 M. The activity of intracellular enzyme was inhibited by Co$^{2+}$, Hg$^{2+}$, Zn$^{2+}$, 0-phenanthroline, $\rho$-CMB, EDTA and iodoacetate, and stimulated by Ca$^{2+}$, L-cysteine and 2-mercaptoethanol. This enzyme was an alginase specifically degrading alginic acid.


Alginase;intracellular enzyme;alginic acid;Vibria sp. AL-145


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