Abstract
β-Glucanase has received great attention in recent years regarding their potential biotechnological applications and antifungal activities. Herein, the specific objectives of the present study were to purify, characterize and immobilize β-glucanase from Aspergillus niger using covalent binding and cross linking techniques. The evaluation of β-glucanase in hydrolysis of different lignocellulosic wastes with subsequent bioethanol production and its capability in biocontrol of pathogenic fungi was investigated. Upon nutritional bioprocessing, β-glucanase production from A. niger EG-RE (MW390925.1) preferred ammonium nitrate and CMC as the best nitrogen and carbon sources, respectively. The soluble enzyme was purified by (NH4)2SO4, DEAE-Cellulose and Sephadex G200 with 10.33-fold and specific activity of 379.1 U/mg protein. Tyrosyl, sulfhydryl, tryptophanyl and arginyl were essential residues for enzyme catalysis. The purified β-glucanase was immobilized on carrageenan and chitosan with appreciable yield. However, the cross-linked enzyme exhibited superior activity along with remarkable improved thermostability and operational stability. Remarkably, the application of the above biocatalyst proved to be a promising candidate in liberating the associate lignocellulosic reducing sugars, which was utilized for ethanol production by Saccharomyces cerevisiae. The purified β-glucanase revealed an inhibitory effect on the growth of two tested phytopathogens Fusarium oxysporum and Penicillium digitatum.
Highlights
Β-Glucanase has received great attention in recent years regarding their potential biotechnological applications and antifungal activities
The following experiments were operated at the 5th day of incubation period, where the highest level of β-glucanase was established. β-glucanase activity and the dry biomass of A. niger were investigated at pH range 4–7 (Fig. 2B)
Β-glucanase productivity by A. niger was maximized through nutritional optimization bioprocess
Summary
Β-Glucanase has received great attention in recent years regarding their potential biotechnological applications and antifungal activities. The specific objectives of the present study were to purify, characterize and immobilize β-glucanase from Aspergillus niger using covalent binding and cross linking techniques. The evaluation of β-glucanase in hydrolysis of different lignocellulosic wastes with subsequent bioethanol production and its capability in biocontrol of pathogenic fungi was investigated. The application of different hydrolytic enzymes, β-glucanase, on many lignocellulosic materials is task for production of bioethanol as a supplier of renewable e nergy[20]. The novelty of this work is presented by production of bioethanol and biocontrol of phytopathogenic fungi using purified fungal β-glucanase. To purify and immobilize the enzyme by covalent-binding and cross-linking techniques. To investigate the capability of β-glucanase in degradation of different lignocellulosic wastes, production of bioethanol and biocontrol of pathogenic fungi
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