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Purification and Some Properties of an Extracellular Pectinase from Bacillus sp. BS-214
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  • Purification and Some Properties of an Extracellular Pectinase from Bacillus sp. BS-214
저자명
Jeon. Beong-Sam,Song. Jae-Young,Lee. Gang-Deog,Kim. Beom-Kyu,Cha. Jae-Young,Lee. Young-Choon
간행물명
Journal of life science
권/호정보
2000년|10권 1호|pp.1-5 (5 pages)
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한국생명과학회
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Pectinase was isolated from culture medium of Bacillus sp. BS-214 and purified 105-fold with 3.4% yield by ammonium sulfate precipitation, gel filteration using Sephadex G-75 and DEAE-cellulose followed by gel filteration through Sephadex G-100. The molecular weight of the purified enzyme was estimated to be about 43 kDa on SDS-PAGE and by gel filtration, indicating that the enzyme is a monomer. the optium pH and temperature of the enzyme were 9.0 and 55$^{circ}C$, respectively. the enzyme was stable at 60$^{circ}C$ for 30min and in a pH range from 7.5 to 10.5 for 12 h ant 4$^{circ}C$. The enzyme activity was highly enhanced by Ca2+, and also K+, Li+ and Na+showed a positive effect, while stongly inhibited by Zn2+ and Hg2+.