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

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 wei...

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Bibliographic Details
Published in:International microbiology 2023-08, Vol.26 (3), p.579-589
Main Authors: Qin, Yongling, Qin, Baoshan, Zhang, Jian, Fu, Yue, Li, Qiqian, Luo, Fengfeng, Luo, Yanmei, He, Haiyan
Format: Article
Language:English
Subjects:
Ammonium
Ammonium sulfate
Anion exchange
Anion exchanging
Applied Microbiology
Aspergillus oryzae
Aspergillus oryzae - metabolism
Biofuels
Biomedical and Life Sciences
Calcium ions
Cellulase
Cellulase - metabolism
Electrophoresis
Endoglucanase
Enzymatic activity
Enzyme activity
Enzyme Stability
Enzymes
Eukaryotic Microbiology
Hot Temperature
Hydrogen-Ion Concentration
Industrial applications
Life Sciences
Medical Microbiology
Microbial Ecology
Microbiology
Molecular weight
pH effects
Pharmaceutical industry
Substrate Specificity
Substrates
Temperature
Zinc
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Summary: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 + , Ca 2+ , and Zn 2+ reduced the catalytic ability of enzyme to the substrate, but Mn 2+ 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.
ISSN:1618-1905
1139-6709
1618-1905
DOI:10.1007/s10123-023-00322-8