논문 상세보기
pp.247-252
고구마 β-아밀라아제를 아세톤 분별침전, DEAE Sephadex A-50, Sephadex G-200으로 정제하였다. 정제효소의 열안정성은 효소농도가 높을수록 높았다. pH 5, 65℃에서 1시간반 후, 효소농도 30㎍/ml 이하에서는 실활하였지만, 100㎍/ml에서는 25%의 활성이 남았다. 정제효소는 pH 4∼10 범위에서 안정하였고, 글리세롤은 pH 안정성을 증가시켰다. NaCl은 pH 4.8, 0.5M 농도에서 효소활성을 100% 저해하였다. SDS는 pH 5, 37℃에서 12시간 반응시킨 결과 0.05% 농도에서 효소활성을 완전히 저해하였다. 염산구아니딘은 pH 5, 37℃에서 13시간 반응시킨 결과 1M 농도에서, 우레아는 8M농도에서 효소활성을 완전히 저해하였다.
β-Amylase was purified from sweet potato by acetone fractionation, Sephadex A-50 ion exchange chromatography and Sephadex G-200 gel chromatography. The higher enzyme concentration was, the higher heat stability of enzyme became. After 1 hour 30 minute. at 60℃ in pH 5, enzyme under concentration of 30 ㎍/ml lost its activity completely and over the concentration of 100 ㎍/ml remained 25% of activity. The enzyme was stabilized at range of pH 4∼10 and pH stability was increased by glycerol. Five moles of NaCl inhibited completely of the enzyme activity. SDS of 0.05% inhibited the enzyme completely after 12 hours at 37℃ in pH 5. One mole guanidine-HCl and 8M urea inhibited the entire enzyme after 13 hours at 37℃ in pH 5.
