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Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366

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논문

Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366

학술지

International microbiology : the official journal of the spanish society for microbiology

저자명

Qin, Yongling; Qin, Baoshan; Zhang, Jian; Fu, Yue; Li, Qiqian; Luo, Fengfeng; Luo, Yanmei; He, Haiyan

초록

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.

발행연도

2023

발행기관

Springer-Verlag

ISSN

1139-6709

ISSN

1618-1905

26

3

페이지

pp.579-589

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1 2023-12-11

논문; 2023-08-01

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