纤维素酶
米曲霉
硫酸铵沉淀
酶
化学
基质(水族馆)
酶分析
色谱法
生物化学
生物
大小排阻色谱法
生态学
作者
Yongling Qin,Qin Bao-shan,Jian Zhang,Yue Fu,Qiqian Li,Fengfeng Luo,Yuling Luo,Hui He
标识
DOI:10.1007/s10123-023-00322-8
摘要
Aspergillus oryzae HML366 is a newly screened cellulase-producing strain. The endoglucanase HML ED1 from A. oryzae HML366 was quickly purified by a two-step method that combines ammonium sulfate precipitation and strong anion exchange column. SDS-PAGE electrophoresis indicated that the molecular weight of the enzyme was 68 kDa. The optimum temperature of the purified endoglucanase was 60 ℃ and the enzyme activity was stable below 70 ℃. The optimum pH was 6.5, and the enzyme activity was stable at pH between 4.5 and 9.0. The analysis indicated that additional Na+, K+, Ca2+, and Zn2+ reduced the catalytic ability of enzyme to the substrate, but Mn2+ enhanced its catalytic ability to the substrate.The Km and Vmax of the purified endoglucanase were 8.75 mg/mL and 60.24 μmol/min·mg, respectively. In this study, we report for the first time that A. oryzae HML366 can produce a heat-resistant and wide pH tolerant endoglucanase HML ED1, which has potential industrial application value in bioethanol, paper, food, textile, detergent, and pharmaceutical industries.
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