English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

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

Del Pozo, M., Fernández-Arrojo, L., Gil, J., Montesinos, A., Golyshina, O., Chernikova, T., et al. (2012). Microbial β-glucosidases from cow rumen metagenome enhance the saccharification of lignocellulose in combination with commercial cellulase cocktail. Biotechnology for Biofuels, 5: 73. doi:10.1186/1754-6834-5-73.

Item is

Files

show Files
hide Files
:
KAL030.pdf (Publisher version), 2MB
Name:
KAL030.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
KAL030s1.zip (Supplementary material), 3MB
Name:
KAL030s1.zip
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/zip / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Del Pozo, MV, Author
Fernández-Arrojo, L, Author
Gil, J, Author
Montesinos, A, Author
Golyshina, OV, Author
Chernikova, TN, Author
Nechitaylo, Taras Y.1, Author           
Waliszek, A, Author
Tortajada, M, Author
Rojas, A, Author
Huws, SA, Author
Newbold, CJ, Author
Polaina, J, Author
Ferrer, M, Author
Golyshin, P, Author
Affiliations:
1Max Planck Research Group Insect Symbiosis, MPI for Chemical Ecology, Max Planck Society, ou_421897              

Content

show
hide
Free keywords: -
 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 (p NPbetaG) and p NP-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 p NPbetaG 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 p NPbetaG). 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.

Details

show
hide
Language(s):
 Dates: 2012-09-142012-09-212012
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: KAL030
DOI: 10.1186/1754-6834-5-73
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biotechnology for Biofuels
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : BioMed Central
Pages: - Volume / Issue: 5 Sequence Number: 73 Start / End Page: - Identifier: ISSN: 1754-6834
CoNE: https://pure.mpg.de/cone/journals/resource/1754-6834