ArticleInternational microbiology : the official journal of the Spanish Society for Microbiology2023
Purification and enzymatic properties of a new thermostable endoglucanase from Aspergillus oryzae HML366.
Article in International microbiology : the official journal of the Spanish Society for Microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 7 citations in OpenAlex.
- Integrated cellulase continuous production and downstream processing using a packed-bed bioreactor for solid-state fermentation by thermophilic fungus.Bioprocess and biosystems engineering · 2026Article
- Fungal cellulases: a comprehensive review on production, innovations, and applications.Archives of microbiology · 2026Review
- Biochemical characterization of a bilfunctional endoglucanase/glucomannanase derived from mountain soil.Biotechnology letters · 2025Article
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8 authors at 3 institutions in 1 country.
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Abstract
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
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