Microbial β-glucosidases from cow rumen metagenome enhance the saccharification of lignocellulose in combination with commercial cellulase cocktail

2.50
Hdl Handle:
http://hdl.handle.net/10033/620703
Title:
Microbial β-glucosidases from cow rumen metagenome enhance the saccharification of lignocellulose in combination with commercial cellulase cocktail
Authors:
Del Pozo, Mercedes V; Fernández-Arrojo, Lucía; Gil-Martínez, Jorge; Montesinos, Alejandro; Chernikova, Tatyana N; Nechitaylo, Taras Y; Waliszek, Agnes; Tortajada, Marta; Rojas, Antonia; Huws, Sharon A; Golyshina, Olga V; Newbold, Charles J; Polaina, Julio; Ferrer, Manuel; Golyshin, Peter N
Abstract:
Abstract Background A complete saccharification of plant polymers is the critical step in the efficient production of bio-alcohols. Beta-glucosidases acting in the degradation of intermediate gluco-oligosaccharides produced by cellulases limit the yield of the final product. Results In the present work, we have identified and then successfully cloned, expressed, purified and characterised 4 highly active beta-glucosidases from fibre-adherent microbial community from the cow rumen. The enzymes were most active at temperatures 45–55°C and pH 4.0-7.0 and exhibited high affinity and activity towards synthetic substrates such as p-nitrophenyl-beta-D-glucopyranoside (pNPbetaG) and pNP-beta-cellobiose, as well as to natural cello-oligosaccharides ranging from cellobiose to cellopentaose. The apparent capability of the most active beta-glucosidase, herein named LAB25g2, was tested for its ability to improve, at low dosage (31.25 units g-1 dry biomass, using pNPbetaG as substrate), the hydrolysis of pre-treated corn stover (dry matter content of 20%; 350 g glucan kg-1 dry biomass) in combination with a beta-glucosidase-deficient commercial Trichoderma reseei cellulase cocktail (5 units g-1 dry biomass in the basis of pNPbetaG). LAB25g2 increased the final hydrolysis yield by a factor of 20% (44.5 ± 1.7% vs. 34.5 ± 1.5% in control conditions) after 96–120 h as compared to control reactions in its absence or in the presence of other commercial beta-glucosidase preparations. The high stability (half-life higher than 5 days at 50°C and pH 5.2) and 2–38000 fold higher (as compared with reported beta-glucosidases) activity towards cello-oligosaccharides may account for its performance in supplementation assays. Conclusions The results suggest that beta-glucosidases from yet uncultured bacteria from animal digestomes may be of a potential interest for biotechnological processes related to the effective bio-ethanol production in combination with low dosage of commercial cellulases.
Citation:
Biotechnology for Biofuels. 2012 Sep 21;5(1):73
Issue Date:
21-Sep-2012
URI:
http://dx.doi.org/10.1186/1754-6834-5-73; http://hdl.handle.net/10033/620703
Type:
Journal Article
Appears in Collections:
Publications of RG Environmental Microbiology (UMW)

Full metadata record

DC FieldValue Language
dc.contributor.authorDel Pozo, Mercedes Ven
dc.contributor.authorFernández-Arrojo, Lucíaen
dc.contributor.authorGil-Martínez, Jorgeen
dc.contributor.authorMontesinos, Alejandroen
dc.contributor.authorChernikova, Tatyana Nen
dc.contributor.authorNechitaylo, Taras Yen
dc.contributor.authorWaliszek, Agnesen
dc.contributor.authorTortajada, Martaen
dc.contributor.authorRojas, Antoniaen
dc.contributor.authorHuws, Sharon Aen
dc.contributor.authorGolyshina, Olga Ven
dc.contributor.authorNewbold, Charles Jen
dc.contributor.authorPolaina, Julioen
dc.contributor.authorFerrer, Manuelen
dc.contributor.authorGolyshin, Peter Nen
dc.date.accessioned2017-01-16T15:28:06Z-
dc.date.available2017-01-16T15:28:06Z-
dc.date.issued2012-09-21en
dc.identifier.citationBiotechnology for Biofuels. 2012 Sep 21;5(1):73en
dc.identifier.urihttp://dx.doi.org/10.1186/1754-6834-5-73en
dc.identifier.urihttp://hdl.handle.net/10033/620703-
dc.description.abstractAbstract Background A complete saccharification of plant polymers is the critical step in the efficient production of bio-alcohols. Beta-glucosidases acting in the degradation of intermediate gluco-oligosaccharides produced by cellulases limit the yield of the final product. Results In the present work, we have identified and then successfully cloned, expressed, purified and characterised 4 highly active beta-glucosidases from fibre-adherent microbial community from the cow rumen. The enzymes were most active at temperatures 45–55°C and pH 4.0-7.0 and exhibited high affinity and activity towards synthetic substrates such as p-nitrophenyl-beta-D-glucopyranoside (pNPbetaG) and pNP-beta-cellobiose, as well as to natural cello-oligosaccharides ranging from cellobiose to cellopentaose. The apparent capability of the most active beta-glucosidase, herein named LAB25g2, was tested for its ability to improve, at low dosage (31.25 units g-1 dry biomass, using pNPbetaG as substrate), the hydrolysis of pre-treated corn stover (dry matter content of 20%; 350 g glucan kg-1 dry biomass) in combination with a beta-glucosidase-deficient commercial Trichoderma reseei cellulase cocktail (5 units g-1 dry biomass in the basis of pNPbetaG). LAB25g2 increased the final hydrolysis yield by a factor of 20% (44.5 ± 1.7% vs. 34.5 ± 1.5% in control conditions) after 96–120 h as compared to control reactions in its absence or in the presence of other commercial beta-glucosidase preparations. The high stability (half-life higher than 5 days at 50°C and pH 5.2) and 2–38000 fold higher (as compared with reported beta-glucosidases) activity towards cello-oligosaccharides may account for its performance in supplementation assays. Conclusions The results suggest that beta-glucosidases from yet uncultured bacteria from animal digestomes may be of a potential interest for biotechnological processes related to the effective bio-ethanol production in combination with low dosage of commercial cellulases.en
dc.titleMicrobial β-glucosidases from cow rumen metagenome enhance the saccharification of lignocellulose in combination with commercial cellulase cocktailen
dc.typeJournal Articleen
dc.language.rfc3066enen
dc.rights.holderDel Pozo et al.; licensee BioMed Central Ltd.en
dc.date.updated2015-09-04T08:30:39Zen
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