논문 상세보기
pp.348-352
과요오드산-산화전분으로 밀 β-amylase(Himaltosin GL. 일본한큐바이오사)를 변형시켜서 인공당단백질을 만들었다. pH 8.0에서 변형한 효소는 비변형효소의 96%. pH 9.7에서 변형한 효소는 17%의 활성이 남았다. 60℃에서의 열안정성은 α-cyclodextrin (α-CD)존재 시에 변형하여 α-CD 존재시에 분석한 효소는 10분 뒤에 비활성의 8%가 남은 반면 변형하지 않은 효소는 5% 밖에 남지 않았다. pH안정성은 변형시켜서 α-CD존재 하에 분석한 효소가 가장 높아서 pH 2∼5와 6∼12에서 안정성이 매우 증가하였다. HPLC 분석 결과 효소는 하나의 피크를 나타냈으며 변형시킨 것은 당결합으로 분자량이 커져서 유출시간이 약간 빨라졌다.
The stabilization of wheat β-amylase(Himaltosin GL, Hankyu-Bio) was attained by modification with periodate-oxidized soluble starch. The specific activities of modified enzyme at pH 9.7 and pH 8.0 were 17% and 96%, respectively, compared with that of native enzyme. The pH stability of modified enzyme was increased at pH 2∼5 and 6∼12 in the presence of α-cyclodextrin(α-CD) compared with that of native enzyme, and optimum pH of the enzyme was changed from pH 5.0 to pH 7.0 by the modification. Thermal stability of the modified enzyme was increased. After treatment at 60℃ for 10min, the activity remained 8% for the enzyme modified at pH 8.0 in the presence of α-CD and tested in the presence of α-CD, 5% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The molecular weight of the modified enzyme was slightly increased in HPLC analysis.
