β-Glucosidase Production by Trichoderma reesei

Juhász, Tamás; Egyházi, Anita; Réczey, Kati

doi:10.1007/978-1-59259-991-2_21

Cited by 12 publications

(10 citation statements)

References 19 publications

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“…Importantly, NPTII-BglC was able to hydrolyze not only pure cellobiose, but also the complex mixture of glucose oligomers produced by enzymatic hydrolysis of tobacco leaf tissue. Commercial cellulase preparations are typically made from the supernatant liquid of Trichoderma reesei cell cultures, which have been shown to contain low levels of b-glucosidase activity relative to their cellulase activities (Juhász et al 2005). Supplementation of commercial cellulases with b-glucosidase has been shown to improve the performance of lab-scale cellulosic ethanol production (e.g., Schell et al 1990;Spindler et al 1989), and may be required for efficient glucose production on a commercial scale.…”

Section: Discussionmentioning

confidence: 99%

“…Typical microbial cellulase systems contain a complex mixture of endo-and exo-glucanases, b-glucosidase, accessory enzymes, and non-hydrolytic proteins for efficient cellulose hydrolysis (reviewed in Zhang and Lynd 2004). The most common industrial source of cellulases is the cell culture supernatant of the fungus Trichoderma reesei, which has a high cellulase activity, but it is often deficient in b-glucosidase activity (Juhász et al 2005). Supplementation of T. reesei cellulase preparations with b-glucosidase increases glucose and/or ethanol concentrations after cellulose hydrolysis (e.g.…”

Section: Introductionmentioning

confidence: 99%

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An efficient downstream box fusion allows high-level accumulation of active bacterial beta-glucosidase in tobacco chloroplasts

et al. 2011

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Production of enzymes for lignocellulose hydrolysis in planta has been proposed as a lower-cost alternative to microbial production, with plastid transformation as a preferred method due to high foreign protein yields. An important regulator of chloroplast protein production is the downstream box (DB) region, located immediately downstream of the start codon. Protein accumulation can vary over several orders of magnitude by altering the DB region. Experiments in bacteria have suggested that these differences in protein accumulation may result from changes in translation efficiency, though the precise mechanism of DB function is not known. In this study, three DB regions were fused to the bglC ORF encoding a β-glucosidase from the thermophilic bacterium Thermobifida fusca and inserted into the tobacco (Nicotiana tabacum) plastid genome. More than a two order of magnitude of difference in BglC protein accumulation was observed, dependent on the identity of the DB fusion. Differential transcript accumulation explained some the observed differences in protein accumulation, but in addition, less 3' degradation of bglC transcripts was observed in transgenic plants that accumulated the most BglC enzyme. Chloroplast-produced BglC was active against both pure cellobiose and against tobacco lignocellulose. These experiments demonstrate the potential utility of transplastomic plants as a vehicle for heterologous β-glucosidase production for the cellulosic ethanol industry.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

An efficient downstream box fusion allows high-level accumulation of active bacterial beta-glucosidase in tobacco chloroplasts

et al. 2011

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“…As an immobilized enzyme, β-glucosidase, is highly beneficial for the beverage industry since it can be used for flavor enrichment of wine and fruit juice (Gallifuoco et al 1998). Previously, the production of β-glucosidase from various fungi has been reported (Juhasz et al 2005;Flachner and Reczey 2004). Lactic acid bacteria and bifidobacteria possessing β-glucosidase activity were used as functional starter cultures in soymilk fermentation to obtain the bioactive isoflavone aglycones, daidzein and genistein (Pyo et al 2005;Tsangalis et al 2002Tsangalis et al , 2003.…”

Section: Introductionmentioning

confidence: 97%

Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Mahajan

Desai

Lele

2010

Food Bioprocess Technol

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Hydrolytic enzymes, viz. α-and β-glucosidase, were produced from indigenous isolate, Lactobacillus acidophilus, isolated from fermented Eleusine coracana. Production of these enzymes was enhanced by optimizing media using one factor at a time followed by response surface methodology. The optimized media resulted in a 2.5-and 2.1-fold increase in α-and β-glucosidase production compared with their production in basal MRS medium. Localization studies indicated 80% of the total activity to be present in the cell membrane-bound fraction. Lack of sufficient release of these enzymes using various physical, chemical, and enzymatic methods confirmed their unique characteristic of being tightly cell membrane bound. Enzyme characterization revealed that both α-and β-glucosidase exhibited optimum catalytic activity at 50°C and pH 6.0 and 5.0, respectively. K m and V max of α-glucosidase were 4.31 mM and 149 μmolmin −1 mL −1 for pnitrophenyl-α-D-glucopyranoside as substrate and 3.8 mM and 120 μmolmin −1 mL −1 for β-glucosidase using p-nitrophenyl-β-D-glucopyranoside as the substrate.

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“…Non-optimized SSF was carried out in Erlenmeyer flasks (250 ml) with 5 g of powdered substrate. The liquid salt medium (LSM) with composition (gL -1 ): (NH4)2SO4, 3.5; KH2PO4, 3; MgSO4.7H2O, 0.05; CaCl2.H2O, 0.05 (Juhasz et al, 2005) was used. The substrate was moistened with distilled water and 5 ml of LSM to give 80% initial moisture and autoclaved at 121°C.…”

Section: Solid State Fermentationmentioning

confidence: 99%

Biohydrolysis of Saccharum spontaneum for cellulase production by Aspergillus terreus

Ilyas¹

2012

Afr.J.Biotechnol

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Saccharum spontaneum, a wasteland weed, is utilized for cellulase production by Aspergillus terreus in solid state fermentation. S. spontaneum served as good carbon source and solid support. Various process parameters including optimal nitrogen source, initial moisture level, incubation time, initial pH, incubation temperature and inoculum size were evaluated. The maximum cellulase production was attained at 70% of initial moisture with incubation of 96 h at 30±2°C, and pH 4.5. Ammonium sulphate in concentration of 0.2% (w/w) was the most preferable nitrogen source among all tested nitrogen sources. The results indicate that S. spontaneum could be utilized as a substrate in solid state fermentation (SSF) for economic production of cellulase.

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β-Glucosidase Production by Trichoderma reesei

Cited by 12 publications

References 19 publications

An efficient downstream box fusion allows high-level accumulation of active bacterial beta-glucosidase in tobacco chloroplasts

An efficient downstream box fusion allows high-level accumulation of active bacterial beta-glucosidase in tobacco chloroplasts

Production of Cell Membrane-Bound α- and β-Glucosidase by Lactobacillus acidophilus

Biohydrolysis of Saccharum spontaneum for cellulase production by Aspergillus terreus

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