A comprehensive analysis of the effects of the main component enzymes of cellulase derived from <i>Trichoderma reesei</i> on biomass saccharification

Kawai, Tetsushi; Nakazawa, Hikaru; Ida, Noriko; Okada, Hirofumi; Ogasawara, Wataru; Morikawa, Yasushi; Kobayashi, Yoshinori

doi:10.1007/s10295-013-1290-6

Cited by 14 publications

(7 citation statements)

References 30 publications

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“…Genomic DNA and RNA isolation Penicillium funiculosum NCL1 was grown in Reese and Mandel medium [18] [14]. Mycelium was collected by filtration using muslin cloth.…”

Section: Maldi-tof and Peptide Mass Fingerprinting (Pmf)mentioning

confidence: 99%

Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization

Ramani

Meera

Vanitha

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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A partial peptide sequence of β-glucosidase isoform (Bgl4) of Penicillium funiculosum NCL1 was identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The cDNA (bgl4) encoding Bgl4 protein was cloned from P. funiculosum NCL1 RNA by consensus RT-PCR. The bgl4 gene encoded 857 amino acids that contained catalytic domains specific for glycoside hydrolase family 3. The cDNA was over-expressed in Pichia pastoris KM71H and the recombinant protein (rBgl4) was purified with the specific activity of 1,354.3 U/mg. The rBgl4 was a glycoprotein with the molecular weight of ~130 kDa and showed optimal activity at pH 5.0 and 60 °C. The enzyme was thermo-tolerant up to 60 °C for 60 min. The rBgl4 was highly active on aryl substrates with β-glucosidic, β-xylosidic linkages and moderately active on cellobiose and salicin. It showed remarkably high substrate conversion rate of 3,332 and 2,083 μmol/min/mg with the substrates p-nitrophenyl β-glucoside and cellobiose respectively. In addition, the rBgl4 showed tolerance to glucose concentration up to 400 mM. It exhibited twofold increase in glucose yield when supplemented with crude cellulase of Trichoderma reesei Rut-C30 in cellulose hydrolysis. These results suggested that rBgl4 is a thermo- and glucose-tolerant β-glucosidase and is a potential supplement for commercial cellulase in cellulose hydrolysis and thereby assures profitability in bioethanol production.

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“…Genomic DNA and RNA isolation Penicillium funiculosum NCL1 was grown in Reese and Mandel medium [18] [14]. Mycelium was collected by filtration using muslin cloth.…”

Section: Maldi-tof and Peptide Mass Fingerprinting (Pmf)mentioning

confidence: 99%

Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization

Ramani

Meera

Vanitha

et al. 2015

Journal of Industrial Microbiology and Biotechnology

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“…EG, CBH, and BGL are the most important components for cellulose hydrolysis and act synergistically to degrade crystalline cellulose to glucose. BGL converts the oligosaccharides produced by EG and CBH into glucose (Kawai et al 2013). Low BGL activity leads to cellobiose accumulation and reduced biomass conversion efficiency (Nakazawa et al 2012).…”

Section: An Evaluation For Saccharification Efficiency Of S Commune mentioning

confidence: 99%

Optimization of Medium Components for β-glucosidase Production in Schizophyllum commune KUC9397 and Enzymatic Hydrolysis of Lignocellulosic Biomass

Lee¹,

Lee²,

Kim³

et al. 2014

BioResources

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Medium components for β-glucosidase (BGL) production in Schizophyllum commune KUC9397 were optimized using a central composite design and response surface methodology. From the various medium components tested, cellulose, soy peptone, and thiamine HCl were selected as the optimal carbon, nitrogen, and vitamin sources, respectively. The highest BGL production was obtained with 2.96% cellulose, 2.30% soy peptone, and 0.11% thiamine HCl. BGL production in the optimized medium was increased 7.2-fold compared to production in an unoptimized medium. Crude enzyme preparation from S. commune KUC9397 was used to saccharify pretreated lignocellulosic biomass. The crude enzyme preparations showed statistically equal saccharification rates as Cellobiase, a commercial BGL. This finding indicates that crude enzymes produced by S. commune KUC9397 have good potential for application in cellulosic biomass conversion systems in place of Cellobiase.

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“…The enzymes exo‐β‐1,4‐glucanase, endo‐β‐1,4‐glucanase and β‐glucosidase are three components of cellulase. The cellulose was completely hydrolyzed to glucose by the combined action of the three enzymes; in the absence of any of these enzymes, cellulose cannot be completely hydrolyzed to glucose . Glucose is a reducing agent, which can inhibit the oxidative degradation of lignin catalyzed by LiP .…”

Section: Resultsmentioning

confidence: 99%

The synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid‐state fermentation substrate on enzyme‐catalyzed oxidative degradation of lignin

Zhang

Wang

Fan

et al. 2019

J of Chemical Tech & Biotech

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BACKGROUND We have reported the oxidative degradation of lignin catalyzed by lignin peroxidase (LiP) from Aspergillus oxyzae broth in previous studies. The aim of the present paper is to obtain the maximal yield of total reducing sugar (Ytrs) by synergistic effect analysis between LiP and three components of cellulase (endo‐β‐1,4‐glucanase, exo‐β‐1,4‐glucanase and β‐glucosidase). RESULTS The Michaelis–Menten analogous model was applied to fit experimental data of lignin oxidative degradation. The apparent Michaelis constant of purified LiP product (3.02 mg mL–1) was lower than that of the crude LiP solution (4.74 mg mL−1), and the apparent maximum reaction rate of the purified LiP product (1.15 mg mL−1 h−1) was higher than that of the crude LiP solution (0.86 mg mL−1 h−1). The maximum Ytrs (49.794%) was obtained when the β‐glucosidase activity was 0; the activities of LiP, endo‐β‐1,4‐glucanase and exo‐β‐1,4‐glucanase were 10.77, 3.360 and 3.427 U mL−1 (3:1:1), respectively. The components and structure of the substrate was extremely different before and after synergistic action under optimal conditions. CONCLUSION A synergistic effect exists between LiP and cellulase. β‐glucosidase is the key enzyme that inhibits the oxidative degradation of lignin. The results lay the foundation for screening and optimizing fermentation process conditions of the LiP strain, and improving the efficiency of enzyme‐catalyzed oxidative degradation of lignin. © 2018 Society of Chemical Industry

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A comprehensive analysis of the effects of the main component enzymes of cellulase derived from Trichoderma reesei on biomass saccharification

Cited by 14 publications

References 30 publications

Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization

Molecular cloning and expression of thermostable glucose-tolerant β-glucosidase of Penicillium funiculosum NCL1 in Pichia pastoris and its characterization

Optimization of Medium Components for β-glucosidase Production in Schizophyllum commune KUC9397 and Enzymatic Hydrolysis of Lignocellulosic Biomass

The synergistic effect of lignin peroxidase and cellulase in Aspergillus oryzae solid‐state fermentation substrate on enzyme‐catalyzed oxidative degradation of lignin

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