ArticleCurrent microbiology2020
Purification and Biochemical Characterization of Alkalophilic Cellulase from the Symbiotic Bacillus subtilis BC1 of the Leopard Moth, Zeuzera pyrina (L.) (Lepidoptera: Cossidae).
Article in Current microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 36 citations in OpenAlex.
- Alkaliphilic microbial cellulases: sources, structural insights, and bioengineering approaches for industrial applications.Archives of microbiology · 2026Review
- Genomic Functional Analysis and Cellulase Characterization for the Enzyme-Producing StrainMicroorganisms · 2025Article
- The Rhizospheric Alkali-Halotolerant Bacillus sp. KhSb-159 Enhanced Growth Parameters of the Mung Bean Crop.Current microbiology · 2025Article
- Characterization of Cellulose-Degrading Bacteria Isolated from Silkworm Excrement and Optimization of Its Cellulase Production.Polymers · 2023Article
- The genome sequence of the Leopard Moth,Wellcome open research · 2023Article
- Expression, characterization, and activity optimization of a novel cellulase from the thermophilic bacteria Cohnella sp. A01.Scientific reports · 2022Article
- Coconut Mesocarp-Based Lignocellulosic Waste as a Substrate for Cellulase Production from High Promising Multienzyme-ProducingMicroorganisms · 2022Article
- Biochemical Characterization of Cellulase FromFrontiers in bioengineering and biotechnology · 2021Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the current study, an extracellular cellulase belonging to symbiotic Bacillus subtilis Bc1 of the leopard moth is purified and characterized. The molecular mass of enzyme was 47.8 kDa using SDS-PAGE. The purified enzyme had optimum activity in temperature and pH around 60 °C and 8, respectively. The purified cellulase was introduced as a stable enzyme in a wide variety of temperature (20-80 °C) and pH (4-10) and remained active to more than 74% at 80 °C for 1 h. Moreover, the cellulase extremely was stabled in the presence of metal ions and organic solvents and its activity was increased by acetone (20% v/v), CaCl
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