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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 (NH 4 ) 2 SO 4 , DEAE-Cellulose and Sephadex G 200  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 .

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Production and immobilization of β-glucanase from Aspergillus niger with its applications in bioethanol production and biocontrol of phytopathogenic fungi