摘要
诺卡氏菌株(Nocaridasp.)82除去菌体的发酵液经硫酸镀沉淀、DEAE-纤维素离子交换层析、SephadexG-200凝胶过滤,得到高纯度的β-淀粉酶。用SDS-PAGE测定酶蛋白分子量为53000,不具亚基;酶反应最适pH和温度分别为7.0和60℃,有较高的热稳定性;Fe2十和Zn2+对酶活力有促进作用,而Hg2+对酶活力有抑制作用。
A thermostableβ-amylase from the culture supernatant of Nocardia sp.82 was purified to PAGE homogenous by ammonium sulfate precipitation DEAE-cellulose column chromatography and sephadex G-200 filtration with 33.02 fold purification and 37.2% recovery. The molecular weight estimated with SDS-PAGE was 53000. The optimum conditions for activity were pH7.0, temperature 60℃, and it remained 40% activi ty at 100℃ (30min). Theβ-amylase was activated by Fe2+、 Zn2+ and it was inhibied by Hg2+.
出处
《河北大学学报(自然科学版)》
CAS
1997年第2期41-45,共5页
Journal of Hebei University(Natural Science Edition)
基金
河北省科委资助