Accessory enzymes influence cellulase hydrolysis of the model substrate and the realistic lignocellulosic biomass

Characterization and production of efficient lignocellulytic enzyme cocktails for biomass conversion is the need for biofuel industry. The present investigation reports the modeling and optimization studies of lignocellulolytic enzyme cocktail production by Cotylidia pannosa under submerged conditions. The predominant enzyme activities of cellulase, xylanase and laccase were produced in the cocktail through submerged conditions using wheat bran as a substrate. A central composite design approach was utilized to model the production process using temperature, pH, incubation time and agitation as input variables with the goal of optimizing the output variables namely cellulase, xylanase and laccase activities. The effect of individual, square and interaction terms on cellulase, xylanase and laccase activities were depicted through the non-linear regression equations with significant R 2 and P-values. An optimized value of 20 U/ml, 17 U/ml and 13 U/ml of cellulase, xylanase and laccase activities, respectively, were obtained with a media pH of 5.0 in 77 h at 31C, 140 rpm using wheatbran as a substrate. Overall, the present study introduces a fungal strain, capable of producing lignocellulolytic enzyme cocktail for subsequent applications in biofuel industry.

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“…14,15 Therefore, more potent adequate enzyme preparations need to be developed for the efficient enzymatic saccharification process.…”

Section: Accellerase® Triomentioning

confidence: 99%

Bioprocessing of wheat bran for the production of lignocellulolytic enzyme cocktail byCotylidia pannosaunder submerged conditions

2016

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“…Therefore, the high conversion efficiency of the secretome of T. harzianum EM0925 might be achieved from its numerously and quantitatively balanced cellulases and hemicellulases. Previously, partial replacement of cellulases with auxiliary enzymes has reduced the required amount of commercial cellulases to achieve high hydrolysis yields [11,44]. Yang et al [45] reported a degree of synergy of 1.35 for the hydrolysis of delignified corn stover when studying the synergistic effect between a commercial enzyme preparation and a bifunctional enzyme consisting of an acetyl xylan esterase and a α-l-arabinofuranosidase.…”

Section: Discussionmentioning

confidence: 99%

“…also have great potential in food and feed industry applications. Therefore, in terms of the whole component utilization of plant cell wall polysaccharides, not only lack of β-glucosidase restricted the efficient conversion of cellulose, the lack of hemicellulase in Trichoderma reesei extracellular proteome also made it difficult to utilize hemicellulose [11]. Hemicellulase activity of commercial cellulase production model strains T. reesei QM6a and T. reesei QM9414 has been determined by Li et al [12], in which the xylanase activity was 5.42 and 1.27 U/mL, while xylosidase activity was only 0.4 and 0.005 U/mL, respectively.…”

Section: Introductionmentioning

confidence: 99%

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Zhang

Yang

Luo

et al. 2020

IJMS

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Fermentable sugars are important intermediate products in the conversion of lignocellulosic biomass to biofuels and other value-added bio-products. The main bottlenecks limiting the production of fermentable sugars from lignocellulosic biomass are the high cost and the low saccharification efficiency of degradation enzymes. Herein, we report the secretome of Trichoderma harzianum EM0925 under induction of lignocellulose. Numerously and quantitatively balanced cellulases and hemicellulases, especially high levels of glycosidases, could be secreted by T. harzianum EM0925. Compared with the commercial enzyme preparations, the T. harzianum EM0925 enzyme cocktail presented significantly higher lignocellulolytic enzyme activities and hydrolysis efficiency against lignocellulosic biomass. Moreover, 100% yields of glucose and xylose were obtained simultaneously from ultrafine grinding and alkali pretreated corn stover. These findings demonstrate a natural cellulases and hemicellulases mixture for complete conversion of biomass polysaccharide, suggesting T. harzianum EM0925 enzymes have great potential for industrial applications.

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“…Screening of phages-host interaction to increase lysis rates precisely (the kinetics exponential decay rate) with a functional lytic enzyme during phage infecting bacterial cells causes bacteriolysis and results in dead but intact bacterial cells (Filatova et al, 2015;Sun et al, 2015). Virolysins lysed cell wall peptidoglycan that yielded to primary amino sugars released and free intracellular components from hydrolyzed bacteria in the reaction qualitatively and quantitatively (Kadurugamuwa et al, 1998;Li et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Potentiality of lytic bacteriophages and their virolysins in lysing multi-drug resistant Salmonella typhi

Elshayeb¹,

Ahmed²,

Siddig³

et al. 2017

Afr. J. Biotechnol.

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Bacteriophage virolysins or lytic enzymes are bacterial peptidoglycan hydrolases responsible for lysing bacterial cells. Consequently, they are used as enzybiotics alongside with bacteriophage therapy to remedy multi-drug resistant Salmonella typhi. The objective of this study was to evaluate the potentiality of lytic bacteriophages and their virolysins in curing multi-drug resistant S. typhi. S. typhi was isolated and identified according to WHO and ISO guidelines. Antibiotics susceptibilities were tested using CLSI recommendations. Correspondingly, bacteriophage-lysing efficiency was assayed by plaques formation using the double-layer agar technique. Virolysins were extracted using ultracentrifugation and purified by dialysis after buffering in ammonium sulfate. Virolysins activity was determined by measuring the reaction mixtures spectrophotometrically (bacteria incubated as substrate in 37°C for 4 h). The phages and virolysins kinetics exponential rates were calculated using specific differential equations. Susceptibility data plotted based on antibiogram criteria confirmed that 33% of S. typhi isolates were multi-drug resistant. For bacteriophage replication and multiplicity of infection, phages were amplified to produce the maximum particles of titers. The phage titration data fit on sonogram revealed exponential decay of S. typhi incubated for 12 h. Meanwhile, the enzyme kinetics exponential decay on double reciprocal plot showed irretrievable relationship of host decay in 4 h. Since phages depend on their lytic cycle in lysing bacterial host, their enzymes have more capability in decaying the host; besides they are safe and time-saving when used in the treatment of antibiotics resistant S. typhi.

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Accessory enzymes influence cellulase hydrolysis of the model substrate and the realistic lignocellulosic biomass

Cited by 132 publications

References 23 publications

Bioprocessing of wheat bran for the production of lignocellulolytic enzyme cocktail byCotylidia pannosaunder submerged conditions

Bioprocessing of wheat bran for the production of lignocellulolytic enzyme cocktail byCotylidia pannosaunder submerged conditions

Low-Cost Cellulase-Hemicellulase Mixture Secreted by Trichoderma harzianum EM0925 with Complete Saccharification Efficacy of Lignocellulose

Potentiality of lytic bacteriophages and their virolysins in lysing multi-drug resistant Salmonella typhi

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