논문 상세보기
pp.144-149
고려인삼(Panax ginseng C.A. Meyer) 잎 중의 가용성 invertase를 탈이온수로 추출한 후 황산암모늄 0, 4∼0.6 포화획분에 의하여 조제하였으며 이의 효소화힉적 성질을 검토한 결과는 다음과 같다. 본 효소의 최적 pH와 온도는 pH 6.0과 40℃ 였으며 pH 6.0∼8.0 범위와 40℃ 이하에서 안정하였다. Protease 및 단백질 변성제 처리에 의하여 활성이 현저히 저하되었으며 glycosidase에 의해서는 저해를 받지 않았다. 본 효소는 sucrose와 inulin 등의 β-fructofuranoside 결합을 가진 기질에 특이적으로 작용하여 전형적인 β-fructofuranosidase의 성질을 나타내었다.
Invertase was extracted from Korean ginseng(Panax ginseng C.A. Meyer) leaf with deionized water, and then prepared by ammonium sulfate(0.4∼0.6 Sat.) fractionation, the enzymological properties of the invertase were investigated, and the results obtained were as follows. The optimum pH and temperature of the enzyme were pH 6.0 and 40℃ respectively. The enzyme was stable in the pH range of pH 6.0 to 8.0, and at the temperature below 40℃. The enzyme was inactivated completely by the treatment with some proteases (pepsin, trypsin, papain and ficin) and protein denaturants(8M urea and 6M guanidine-HCl), but not with glycosidases(α-amylase, β-amylase and glucoamylase). The enzyme catalyzed specifically the hydrolization of the β-fructofuranosides such as sucrose and inulin.
