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RISS 인기검색어
- 검색키워드
- 저자 : Hyoung Cchurl Bae (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
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Bae, Hyoung-Cchurl,Choi, Jong-Woo,Nam, Myoung-Soo Korean Society for Food Science of Animal Resource 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius CNU27 possessed a high level of ${\alpha}$-galactosidase activity. Purified ${\alpha}$-galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher than that in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum temperature and pH for the enzyme were $40^{\circ}C$ and 6.0, respectively. The enzyme was stable between 25 and $50^{\circ}C$. However, ${\alpha}$-galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30% of the original activity by addition of $Cu^{2+}$ and $Hg^{2+}$, respectively. Other metal compounds did not affect the enzyme activity significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysis was measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at $40^{\circ}C$.
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Hyoung Cchurl Bae,Jong Woo Choi,Myoung Soo Nam 한국축산식품학회 2007 한국축산식품학회지 Vol.27 No.1
Lactobacillus salivarius subsp. salivarius CNU27 posessed a high level of α-galactosidase activity. Purified α-galactosi-dase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchangechromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher thanthat in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum tempera-ture and pH for the enzyme were 40oC and 6.0, respectively. The enzyme was stable between 25 and 50oC. However, α-galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30%of the original activity by addition of Cu2+ and Hg2+significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysiswas measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at 40oC.
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