ArticleMolecules (Basel, Switzerland)2012
Cloning, purification, and characterization of a heat- and alkaline-stable endoglucanase B from Aspergillus niger BCRC31494.
Article in Molecules (Basel, Switzerland), 2012. 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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8 citing papers in PubMed.
- The development of activity-based mannanase probes.Chemical science · 2026Article
- Adaptation strategies in haloalkaliphilic fungi: Aspergillus salinarum, cladosporium sphaerospermum, and penicillium camemberti.BMC microbiology · 2025Article
- Alkaliphilic/Alkali-Tolerant Fungi: Molecular, Biochemical, and Biotechnological Aspects.Journal of fungi (Basel, Switzerland) · 2023Review
- Production and immobilization of β-glucanase from Aspergillus niger with its applications in bioethanol production and biocontrol of phytopathogenic fungi.Scientific reports · 2021Article
- Efficient enzymatic saccharification of macroalgal biomass using a specific thermostable GH 12 endoglucanase from Aspergillus terreus JL1.World journal of microbiology & biotechnology · 2019Article
- Functional Expression of a Thermostable Endoglucanase from Thermoascus aurantiacus RCKK in Pichia pastoris X-33 and Its Characterization.Molecular biotechnology · 2018Article
- Recombinant expression of thermostable processiveBiotechnology for biofuels · 2017Article
- Genome-wide characterization of cellulases from the hemi-biotrophic plant pathogen,Biotechnology for biofuels · 2017Article
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3 authors.
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Abstract
Endoglucanase B (EGLB) derived from Aspergillus niger BCRC31494 has been used in the food fermentation industry because of its thermal and alkaline tolerance. It was cloned and expressed in Pichia pastoris. According to sequence analysis, the gene open reading frame comprises 1,217 bp with five introns (GenBank GQ292753). According to sequence and protein domain analyses, EGLB was assigned to glycosyl hydrolase family 5 of the cellulase superfamily. Several binding sites were found in the promoter region. The purified recombinant enzyme was induced by 0.5% methanol, and it exhibited optimal activity at 70 °C and pH 4. EGLB was stable for 3 h at temperatures below 60 °C, with more than 90% of its activity remaining. The enzyme was specific for substrates with β-1,3 and β-1,4 linkages. In Lineweaver-Burk plot analysis, the K(m) and V(max) values of EGLB for β-D-glucan were 134 mg/mL and 4.68 U/min/mg, respectively. The enzyme activity was increased by 1.86-fold by Co²⁺ and by 2-fold by Triton X-100 and Tween 80. These favorable properties make EGLB a potential candidate for use in laundry and textile industrial applications.
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