Abstract:Enzyme immobilization is a powerful tool not only as a protective agent against harsh reaction conditions but also for the enhancement of enzyme activity, stability, reusability, and for the improvement of enzyme properties as well. Herein, immobilization of β-glucosidase from Thermotoga maritima (tm-β-Glu) on magnetic nanoparticles (Mnps) functionalized with chitin (ch) was investigated. This technology showed a novel thermostable chitin-binding domain (Tt-ChBD), which is more desirable in a wide range of lar… Show more
“…At the optimal conditions, the remained activity of cross-linked β-glucanase was better than that of carrageenan-immobilized enzyme throughout 8 cycles. The reduction of β-glucanase activity throughout the 8 cycles might be ascribed to protein damage, protein deactivation, and physical damage of the immobilized beads-bound protein 13 , 35 . Figure 6 Reuse of immobilized β-glucanase from A. niger .…”
Section: Resultsmentioning
confidence: 99%
“…So, the optimization of different culture conditions for improving β-glucanase production is of immense interest but the enzymatic processes have unfavorable drawbacks including sensitivity to harsh environmental conditions, difficulties during regeneration as well as recycling processes. Immobilization allows the enzyme to conquer harsh conditions and offer a vital area of study in the field of industrial biotechnology 11 – 13 . Furthermore, immobilization enables enzymes to work with great catalytic activity and consequently diminish the budget of enzymatic processes 12 – 15 .…”
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.
“…At the optimal conditions, the remained activity of cross-linked β-glucanase was better than that of carrageenan-immobilized enzyme throughout 8 cycles. The reduction of β-glucanase activity throughout the 8 cycles might be ascribed to protein damage, protein deactivation, and physical damage of the immobilized beads-bound protein 13 , 35 . Figure 6 Reuse of immobilized β-glucanase from A. niger .…”
Section: Resultsmentioning
confidence: 99%
“…So, the optimization of different culture conditions for improving β-glucanase production is of immense interest but the enzymatic processes have unfavorable drawbacks including sensitivity to harsh environmental conditions, difficulties during regeneration as well as recycling processes. Immobilization allows the enzyme to conquer harsh conditions and offer a vital area of study in the field of industrial biotechnology 11 – 13 . Furthermore, immobilization enables enzymes to work with great catalytic activity and consequently diminish the budget of enzymatic processes 12 – 15 .…”
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.
“…Additionally, it ensures the mechanical stability and good adherence to surfaces of the enzyme layer. Enzyme immobilization in chitosan was achieved by adsorption, encapsulation (e.g., in chitosan beads), cross-linking with various linkers (mainly with glutaradehyde), covalent binding [ 124 ], as well as by affinity [ 125 ] for various biotechnology, industrial or analytical applications [ 124 ].…”
Section: Effect Of the Immobilization Methods And Permselective Membranesmentioning
Enzymatic biosensors enjoy commercial success and are the subject of continued research efforts to widen their range of practical application. For these biosensors to reach their full potential, their selectivity challenges need to be addressed by comprehensive, solid approaches. This review discusses the status of enzymatic biosensors in achieving accurate and selective measurements via direct biocatalytic and inhibition-based detection, with a focus on electrochemical enzyme biosensors. Examples of practical solutions for tackling the activity and selectivity problems and preventing interferences from co-existing electroactive compounds in the samples are provided such as the use of permselective membranes, sentinel sensors and coupled multi-enzyme systems. The effect of activators, inhibitors or enzymatic substrates are also addressed by coupled enzymatic reactions and multi-sensor arrays combined with data interpretation via chemometrics. In addition to these more traditional approaches, the review discusses some ingenious recent approaches, detailing also on possible solutions involving the use of nanomaterials to ensuring the biosensors’ selectivity. Overall, the examples presented illustrate the various tools available when developing enzyme biosensors for new applications and stress the necessity to more comprehensively investigate their selectivity and validate the biosensors versus standard analytical methods.
“…Recently a research was carried out on β-glucosidase obtained from Thermotoga maritima (Tm-β-Glu) and it was functionally immobilized on magnetic nanoparticles (MNPs) with chitin (Ch), this research shows that the novel thermostable chitin-binding domain had the highest binding capacity and Galacto-oligosaccharide synthesis when it was compared with native production of enzyme. In addition, magnetic separation technology have been successfully used in recycling the immobilized β-glucosidase for repetitive batch-wise Galacto-oligosaccharide without significant reduction or loss of enzyme activity ( Alnadari et al, 2020 ). Similarly, another investigation was carried out on thermostable β-glucosidase (Tpebgl3) of Thermotoga petrophila it was immobilized on macro-porous resin modified with polyethyleneimine and glutaraldehyde.…”
Section: Strategies To Enhance Thermostability and Specific Activity Of Cellulase And Xylanase Of Thermophilesmentioning
The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.
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