Please use this identifier to cite or link to this item:
https://hdl.handle.net/10321/5747
Title: | Biochemical and in silico structural properties of a thermo-acid stable β-glucosidase from Beauveria bassiana | Authors: | Magwaza, Buka Amobonye, Ayodeji Bhagwat, Prashant Pillai, Santhosh |
Keywords: | Beauveria bassiana;Enzyme purification;In silico;Molecular docking;Structural elucidation;β-glucosidase | Issue Date: | Apr-2024 | Publisher: | Elsevier BV | Source: | Magwaza, B. et al. 2024. Biochemical and in silico structural properties of a thermo-acid stable β-glucosidase from Beauveria bassiana. Heliyon. 10(7): 1-11. doi:10.1016/j.heliyon.2024.e28667 | Journal: | Heliyon; Vol. 10, Issue 7 | Abstract: | β-glucosidase hydrolyses the glycosidic bonds in cellobiose and cello-oligosaccharides, a critical step in the saccharification for biofuel production. Hence, the aim of this study was to gain insights into the biochemical and structural properties of a β-glucosidase from Beauveria bassiana, an entomopathogenic fungus. The β-glucosidase was purified to homogeneity using salt precipitation, ultrafiltration, and chromatographic techniques, attaining a specific activity of 496 U/mg. The molecular mass of the enzyme was then estimated via SDS-PAGE to be 116 kDa, while its activity pattern was confirmed by zymography using 4-methylumbelliferyl-β-d-glucopyranoside. Furthermore, the pH optima and temperature of the enzyme were found to be pH 5.0 and 60 °C respectively; its activity was significantly enhanced by Mg2+ and Na+ and was found to be relatively moderate in the presence of ethanol and dichloromethane. Molecular docking of the modelled B. bassiana β-glucosidase structure with the substrates, viz., 4-nitrophenyl β-d-glucopyranoside and cellobiose, revealed the binding affinity energies of -7.2 and -6.2 (kcal mol-1), respectively. Furthermore, the computational study predicted Lys-657, Asp-658, and Arg-1000 as the core amino acid residues in the catalytic site of the enzyme. This is the first investigation into a purified β-glucosidase from B. bassiana, providing valuable insights into the functional properties of carbohydrases from entomopathogenic fungal endophytes. |
URI: | https://hdl.handle.net/10321/5747 | ISSN: | 2405-8440 | DOI: | 10.1016/j.heliyon.2024.e28667 |
Appears in Collections: | Research Publications (Applied Sciences) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Heliyon Copyright Clearance.docx | 170.69 kB | Microsoft Word XML | View/Open | |
Magwaza et al_2024.pdf | 4 MB | Adobe PDF | View/Open |
Page view(s)
30
checked on Feb 9, 2025
Download(s)
7
checked on Feb 9, 2025
Google ScholarTM
Check
Altmetric
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.