Enzymatic hydrolysis of steam-pretreated lignocellulosic materials with Trichoderma atroviride enzymes produced in-house
(2009) In Biotechnology for Biofuels 2.- Abstract
- Background: Improvement of the process of cellulase production and development of more efficient lignocellulose-degrading enzymes are necessary in order to reduce the cost of enzymes required in the biomass-to-bioethanol process. Results: Lignocellulolytic enzyme complexes were produced by the mutant Trichoderma atroviride TUB F-1663 on three different steam-pretreated lignocellulosic substrates, namely spruce, wheat straw and sugarcane bagasse. Filter paper activities of the enzymes produced on the three materials were very similar, while beta-glucosidase and hemicellulase activities were more dependent on the nature of the substrate. Hydrolysis of the enzyme preparations investigated produced similar glucose yields. However, the enzymes... (More)
- Background: Improvement of the process of cellulase production and development of more efficient lignocellulose-degrading enzymes are necessary in order to reduce the cost of enzymes required in the biomass-to-bioethanol process. Results: Lignocellulolytic enzyme complexes were produced by the mutant Trichoderma atroviride TUB F-1663 on three different steam-pretreated lignocellulosic substrates, namely spruce, wheat straw and sugarcane bagasse. Filter paper activities of the enzymes produced on the three materials were very similar, while beta-glucosidase and hemicellulase activities were more dependent on the nature of the substrate. Hydrolysis of the enzyme preparations investigated produced similar glucose yields. However, the enzymes produced in-house proved to degrade the xylan and the xylose oligomers less efficiently than a commercial mixture of cellulase and beta-glucosidase. Furthermore, accumulation of xylose oligomers was observed when the TUB F-1663 supernatants were applied to xylan-containing substrates, probably due to the low beta-xylosidase activity of the enzymes. The efficiency of the enzymes produced in-house was enhanced by supplementation with extra commercial beta-glucosidase and beta-xylosidase. When the hydrolytic capacities of various mixtures of a commercial cellulase and a T. atroviride supernatant produced in the lab were investigated at the same enzyme loading, the glucose yield appeared to be correlated with the beta-glucosidase activity, while the xylose yield seemed to be correlated with the beta-xylosidase level in the mixtures. Conclusion: Enzyme supernatants produced by the mutant T. atroviride TUB F-1663 on various pretreated lignocellulosic substrates have good filter paper activity values combined with high levels of beta-glucosidase activities, leading to cellulose conversion in the enzymatic hydrolysis that is as efficient as with a commercial cellulase mixture. On the other hand, in order to achieve good xylan conversion, the supernatants produced by the mutant have to be supplemented with additional beta-xylosidase activity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1518513
- author
- Kovacs, Krisztina LU ; Macrelli, Stefano LU ; Szakacs, George and Zacchi, Guido LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biotechnology for Biofuels
- volume
- 2
- publisher
- BioMed Central (BMC)
- external identifiers
-
- wos:000272094000001
- scopus:68449090624
- pmid:19580644
- ISSN
- 1754-6834
- DOI
- 10.1186/1754-6834-2-14
- language
- English
- LU publication?
- yes
- id
- 21a51747-2ba6-4e2a-8baa-8c01efe9b12e (old id 1518513)
- date added to LUP
- 2016-04-01 13:28:16
- date last changed
- 2023-11-27 06:18:54
@article{21a51747-2ba6-4e2a-8baa-8c01efe9b12e,
abstract = {{Background: Improvement of the process of cellulase production and development of more efficient lignocellulose-degrading enzymes are necessary in order to reduce the cost of enzymes required in the biomass-to-bioethanol process. Results: Lignocellulolytic enzyme complexes were produced by the mutant Trichoderma atroviride TUB F-1663 on three different steam-pretreated lignocellulosic substrates, namely spruce, wheat straw and sugarcane bagasse. Filter paper activities of the enzymes produced on the three materials were very similar, while beta-glucosidase and hemicellulase activities were more dependent on the nature of the substrate. Hydrolysis of the enzyme preparations investigated produced similar glucose yields. However, the enzymes produced in-house proved to degrade the xylan and the xylose oligomers less efficiently than a commercial mixture of cellulase and beta-glucosidase. Furthermore, accumulation of xylose oligomers was observed when the TUB F-1663 supernatants were applied to xylan-containing substrates, probably due to the low beta-xylosidase activity of the enzymes. The efficiency of the enzymes produced in-house was enhanced by supplementation with extra commercial beta-glucosidase and beta-xylosidase. When the hydrolytic capacities of various mixtures of a commercial cellulase and a T. atroviride supernatant produced in the lab were investigated at the same enzyme loading, the glucose yield appeared to be correlated with the beta-glucosidase activity, while the xylose yield seemed to be correlated with the beta-xylosidase level in the mixtures. Conclusion: Enzyme supernatants produced by the mutant T. atroviride TUB F-1663 on various pretreated lignocellulosic substrates have good filter paper activity values combined with high levels of beta-glucosidase activities, leading to cellulose conversion in the enzymatic hydrolysis that is as efficient as with a commercial cellulase mixture. On the other hand, in order to achieve good xylan conversion, the supernatants produced by the mutant have to be supplemented with additional beta-xylosidase activity.}},
author = {{Kovacs, Krisztina and Macrelli, Stefano and Szakacs, George and Zacchi, Guido}},
issn = {{1754-6834}},
language = {{eng}},
publisher = {{BioMed Central (BMC)}},
series = {{Biotechnology for Biofuels}},
title = {{Enzymatic hydrolysis of steam-pretreated lignocellulosic materials with Trichoderma atroviride enzymes produced in-house}},
url = {{http://dx.doi.org/10.1186/1754-6834-2-14}},
doi = {{10.1186/1754-6834-2-14}},
volume = {{2}},
year = {{2009}},
}