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

Abstract

Abstractβ-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.

Aspergillus tamarii mediated green synthesis of magnetic chitosan beads for sustainable remediation of wastewater contaminants

“…53 , 54 . Such primary identification of fungal strain was affirmed by sequencing its internal transcribed spacer (ITS-rDNA) segment 28 , 55 . The fungal genomic DNA was extracted according to 56 .…”

From Cancer Therapy to Winemaking: The Molecular Structure and Applications of β-Glucans and β-1, 3-Glucanases

“…Typical optimal pH values for β-1,3-glucanase activity are on the slightly acidic range of 5.0 to 6.5, but can range anywhere between 4.0 (e.g., fungi Lentinula edodes [ 78 ]) and 9.0 (e.g., armyworm Spodoptera frugiperda [ 79 ]). Fungal β-1,3-glucanases seem to be particularly active on lower pH values (4.0–6.0) [ 77 , 78 , 80 ]. As with most CAZymes, the optimal temperatures for β-1,3-glucanase activity fall within a wide range, with the lowest temperature values belonging to the β-1,3-glucanases of Aspergillus fumigates (24–40 °C) and the highest to the β-1,3-glucanases of archaea Pyrococcus furiosus (100–105 °C) [ 74 , 81 ].…”

“…Much like their natural substrates, β-1,3-glucanases have found a number of applications in many industrial processes and serve as inspiration for several biotechnological solutions. They have been extensively studied for the use in the conversion of β-1,3-glucan containing lignocellulosic biomass, namely of algal origin, into fermentable sugars to be used in bioethanol production [ 80 , 254 ]. They offer a more ecological and energy -efficient alternative to classical methods such as chemical extraction at high temperatures, although the costs of producing the enzymes at a large scale are currently prohibitive [ 255 ].…”

“…Given that β-1,3-glucans are major components of the fungal cell wall, β-1,3-glucanases possess an important antifungal activity. As such, they have attracted a great deal of attention as potential non-chemical biocontrol agents against fungal pathogens in crops [ 70 , 80 ]. Members of the genus Trichoderma are especially well known for their mycoparasitic activities against various phytopathogenic fungi.…”

Facile Cellulase Immobilisation on Bioinspired Silica

“…Immobilisation techniques exploit a covalent or non-covalent bonding such as electrostatic interactions [21,22]. As far as the covalent bonding is concerned, bifunctional coupling agents are used to tether enzymes on supports [23,24]. Concerning the non-covalent bonding, electrostatic interactions, which depend on the charge of the support and the isoelectric point of the enzyme [25][26][27][28], give rise to weak bonds between the support and the enzyme.…”