Industrial Applications of Endoglucanase Obtained from Novel and Native Trichoderma atroviride

Şahin, Selmihan; Özmen, İsmail; Bıyık, Halil

doi:10.15255/cabeq.2014.2130

Cited by 13 publications

(4 citation statements)

References 55 publications

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“…Endoglucanase activity enhancement with azoTAB towards p-nitrophenol-based substrate is significantly higher than avicel microcrystalline substrate. The degree of activity enhancement of endoglucanase is substrate specific as reported by others, 31,38 and our study also shows the difference between a soluble artificial substrate and an insoluble natural substrate. Nearly identical reaction velocities were obtained with in situ light illumination from visible to UV light and in reverse order.…”

Section: Resultssupporting

confidence: 88%

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Improved Activity and Kinetics of Endoglucanase Biofuel Enzyme with Addition of an AzoTAB Surfactant

Seidel,

Ted Lee

2023

Preprint

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Endoglucanases degradeβ-1,4-glycosidic bonds of crystalline cellulose into insoluble or soluble cellooligosaccharides at the solid-liquid interface. The enhanced activity and kinetics of endoglucanase fromAspergillus nigerwith addition of a light responsive azobenzene trimethyl ammonium bromide (azoTAB) surfactant is studied. AzoTAB is a photoresponsive surfactant that exists as a relatively-hydrophobictransisomer under visible light (434 nm) and a relatively-hydrophiliccisisomer under UV light (350 nm). Endoglucanase catalytic activity can be controlled with light illumination slightly for microcrystalline cellulose natural substate (∼15%) and significantly for p-nitrophenol-based model substrate (∼2-fold) by switching between thetrans(higher enzyme binding affinity, resulting higher enzyme unfolding) andcisform of azoTAB. Endoglucanase activity increases 45% towards avicel crystalline substate and 4-fold towards 4-nitrophenyl β-D-cellobioside substrate in the presence of 0.4 mM azoTAB under UV light (90%cisand 10%transisomers). In comparison, endoglucanase catalytic activity increases 5-10% towards crystalline cellulose substrate with the addition of sodium dodecyl benzene sulfonate (SDBS), sodium dodecyl sulfate (SDS) and dodecyl trimethyl ammonium (DTAB). 0.4 mM AzoTAB-UV addition leads to an increase of maximum endoglucanase adsorption (Emax) from 7.89 mg enzyme/g avicel to 12.92 mg enzyme/g avicel and catalytic enzyme efficiency (kcat/KM) from 0.031 L/(mg.s) to 0.061 L/(mg.s). It is found that adsorbed enzyme concentration on substrate correlates to enzyme specific activity for azoTAB containing reaction. Additionally, 40-50% activity enhancement and increased bound enzyme to substrate are detected with azoTAB addition at different enzyme, substrate, and inhibitor concentrations. Improvement of substrate properties of azoTAB addition is associated with lower reciprocal terms of Michaelis constant (KM), the adsorption coefficient (Kad) and fractal parameter (h) values similar to the presence of other surfactants in this study and the literature. Furthermore, 45-50% activity enhancement via azoTAB surfactant preserved for all three cellulase enzyme mixture of endoglucanase, cellohydrolase andβ-glucosidase. Consequently, azoTAB can be applied as profitable additive for the heterogenous enzymatic cellulose hydrolysis, resulting in a 30% decrease in the enzyme load based on the specific activity, adsorption, and fractal kinetics results.

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Section: Resultssupporting

confidence: 88%

“…6 Similarly, azoTAB addition shows 20-30% of endoglucanase catalytic activity enhancement at the 1.5-2 mM surfactant concentration range. In literature, Tween 20 (35%), 30 Tween 80 (27%-34%) 31,32 and Triton X-100 (23%) 31 chemical surfactants have been reported to result in 23-35% endoglucanase activity increases.…”

Section: Resultsmentioning

confidence: 99%

Improved Activity and Kinetics of Endoglucanase Biofuel Enzyme with Addition of an AzoTAB Surfactant

Seidel,

Ted Lee

2023

Preprint

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“…Submerged fermentation is the widely used method for commercial production of cellulases due to the easy recovery of extracellular enzymes, although submerged fermentation can result in reduction of enzyme activity and dilution of enzymes [53]. In the current study the A.oryzae mutant 60(5) was grown in 10 L fermenters under submerged conditions and maximum enzyme units obtained were 913 U dl -1 by using Raw Maize Starch as carbon source (2% w/v).…”

Section: Discussionmentioning

confidence: 98%

Gamma Rays Mediated Mutagenesis of Super Koji (Aspergillus oryzae) to enhance the Thermostability and Production of CMCases: Process Scale-up at Pilot Level

Zeb¹,

Rashid²,

Aleem³

et al. 2019

Preprint

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Background The β-1, 4-endoglucanase belongs to cellulases group of enzymes, which hydrolyse β-1, 4 glucosidic bonds in the naturally occurring cellulose or synthetic Carboxymethyl cellulose CMC thus also named as CMCase. Endoglucanase from Aspergillus oryzae is favoured in food and feed industries due to its GRAS (generally regarded as safe) status and for relatively stable enzymes production. Results Current report is novel as it deals with the development of super Koji strain having hyper production of thermostable CMCases. Hence, the potent Koji’s mutant, hyper producer of thermostable endoglucanase was screened from the available mutants stock (Total = 52 variants), which was generated through gamma rays treatment of Super Koji strain (A. oryzae cmc1). Initially, seventeen (17) mutants hyper producer of CMCases were selected based on the basis of clearance zone index (CI) on the plates supplemented with 1% CMC. Afterwards, six mutants resistant to 2-deoxy-D-glucose were selected having enhanced CMCase production. Mutants’ next screening was on submerged CMCase production. Potent mutant 60(5) having 60 kRad γ-rays exposure showed 3.6 folds hyper CMCase production (6.02 U ml-1). The half-life of endoglucanse produce of A. oryzae mutant 60(5) was 29.42 min and 14.8 min at 55 ⁰C and 60 ⁰C, respectively, which was 4 folds higher than the control at 60 ⁰C. The LC-MS analysis showed that A. oryzae mutant 60(5) does not produce aflatoxins. Field Emission Scanning Electron Microscopy (FESM) of mutated Koji depicted that gamma radiations enhanced the stiffness of fungal mycelia. Kinetics of CMCase production by mutant 60(5) in 10 L and 200L fermenter was as: CMCase = 913 U dl-1 & 821 U dl-1; Specific growth (µ) = 0.064 & 0.082 hours; Cell mass doubling time (td) = 10.71 & 8.42 hours; Yield coefficient with respect to cell mass (Yp/x) = 59 Ug-1 & 89 U g-1 and Specific rate of CMCase production (qp) = 3.84 Ug-1h-1 & 7.37 Ug-1h-1 respectively. Conclusion We concluded, γ-rays induced potent mutations in mutant 60(5) resulting in hyper production of thermostable endoglucanase, which can withstand harsh industrial conditions. Hence, has great potential for applications in food & feed and other industrial processes.

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“…Enzyme activity was ceased by keeping the samples at 80 °C for about 10 min. The samples were then carefully washed with tap water and left at room temperature for drying ( Sahin et al, 2016 ).…”

Section: Methodsmentioning

confidence: 99%

Purification, characterization and thermodynamic analysis of cellulases produced from Thermomyces dupontii and its industrial applications

Nisar

Abdullah

Kaleem

et al. 2022

Saudi Journal of Biological Sciences

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Industrial Applications of Endoglucanase Obtained from Novel and Native Trichoderma atroviride

Cited by 13 publications

References 55 publications

Improved Activity and Kinetics of Endoglucanase Biofuel Enzyme with Addition of an AzoTAB Surfactant

Improved Activity and Kinetics of Endoglucanase Biofuel Enzyme with Addition of an AzoTAB Surfactant

Gamma Rays Mediated Mutagenesis of Super Koji (Aspergillus oryzae) to enhance the Thermostability and Production of CMCases: Process Scale-up at Pilot Level

Purification, characterization and thermodynamic analysis of cellulases produced from Thermomyces dupontii and its industrial applications

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