Date nawah powder as a promising waste for β-mannanase production from a new isolate Aspergillus niger MSSFW, statistically improving production and enzymatic characterization.

Autor: Saleh SAA; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki 12622, Cairo, Egypt., Mostafa FA; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki 12622, Cairo, Egypt., Ahmed SA; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki 12622, Cairo, Egypt. Electronic address: sa.sayed@nrc.sci.eg., Zaki ER; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt., Salama WH; Molecular Biology Department, National Research Centre, Dokki, Cairo, Egypt., Abdel Wahab WA; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki 12622, Cairo, Egypt.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Oct; Vol. 277 (Pt 3), pp. 134447. Date of Electronic Publication: 2024 Aug 02.
DOI: 10.1016/j.ijbiomac.2024.134447
Abstrakt: β-Mannanase producing fungus was isolated from coffee powder waste and identified as Aspergillus niger MSSFW (Gen Bank accession number OR668928). Dates nawah powder as industrial and agricultural waste was the most inducer of β-mannanase production. The Plackett-Burman and Central Composite designs were used to improve β-mannanase titer. Optimization studies enhanced the enzyme yield with approximate 13.50-times. β-Mannanase was purified by Sephadex G-150 gel filtration column and the molecular weight was estimated to be 60 kDa by SDS-PAGE. Crude and purified β-mannanase displayed maximum activity at temperature 60 °C and 50 °C, respectively. Crude β-mannanase showed an activation energy value 2.35-times higher than the purified enzyme. Activation energy for thermal denaturation of the purified β-mannanase was 1.08-times higher than that of the crude enzyme. Purified β-mannanase exhibited higher deactivation rate constant (Kd) and lower half-life (t 0.5 ) and decimal reduction time (D-value) compared with the crude enzyme. Thermodynamic parameters of enthalpy, entropy, and free energy values for crude and purified β-mannanase were calculated. Substrate kinetic parameters suggested that the purified β-mannanase had a strong affinity toward locust bean gum by showing 3.44-times lower Km and 1.99-times higher Vmax compared to the crude enzyme.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. Samia A. Ahmed reports was provided by National Research Centre.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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