Pseudomonas alcaligenes JCL-43이 생산하는 Carrageenase의 정제 및 특성

Purification and Characterization of Carrageenase from Pseudomonas alcaligenes JCL-43

  • 주동식 (강릉대학교 동해안해양생물자원연구센터) ;
  • 조순영 (강릉대학교 동해안해양생물자원연구센터) ;
  • 이정석 (부경대학교 식품공학과) ;
  • 이응호 (부경대학교 식품공학과) ;
  • 양승택 (경성대학교 식품공학과)
  • 발행 : 1999.08.01

초록

Our works performed for preparation of oligosaccharides from carrageenan, seaweed polysaccharide, and one active strain for carrageenan was isolated from sea water and identified to Pseudomonas alcaligenes. Carrageenan degrading enzyme was purified from the culture fluid of isolated strain-Pseudomonas alcaligenes JCL-43, by DEAE-Cellulose, Sephadex G-100, Q-Sepharose and CM Sepharose CL-6B column chromatography. Two enzyme-F-I, F-II- was identified this purifying process, and the molecular weight of the purified carrageenase were estimated to be 23.6kDa and 30.2kDa, respectively. The optimum pH and temperature for two carrageenase activity were 7.0 and 4$0^{\circ}C$. These enzymes were stable in the pH range of 6.0~7.5 and lower than 5$0^{\circ}C$, and required 1.5% NaCl for optimum activity. And these carragennase were inhibited by metal ions such as Cu2+, Zn2+, Hg2+, but increased by Ba2+ and Ca2+, and showed specificity on -carrageenan.

키워드

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