- Pseudomonas alcaligenes JCL-43이 생산하는 Carrageenase의 정제 및 특성
- ㆍ 저자명
- 주동식,조순영,이정석,이응호,양승택
- ㆍ 간행물명
- 생명과학회지
- ㆍ 권/호정보
- 1999년|9권 4호|pp.414-422 (9 pages)
- ㆍ 발행정보
- 한국생명과학회
- ㆍ 파일정보
- 정기간행물| PDF텍스트
- ㆍ 주제분야
- 기타
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.