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Relatively high-substrate consistency hydrolysis of steam-pretreated sweet sorghum bagasse at relatively low cellulase loading.

Authors :
Shen F
Zhong Y
Saddler JN
Liu R
Source :
Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2011 Oct; Vol. 165 (3-4), pp. 1024-36. Date of Electronic Publication: 2011 Jul 05.
Publication Year :
2011

Abstract

Sweet sorghum bagasse (SSB) was steam pretreated in the conditions of 190 °C for 5 min to assess its amenability to the pretreatment and enzymatic hydrolysis. Results showed that pretreatment conditions were robust enough to pretreat SSB with maximum of 87% glucan and 72% xylan recovery. Subsequent enzymatic hydrolysis showed that the pretreated SSB at 2% substrate consistency resulted in maximum of 70% glucan-glucose conversion. Increasing substrate consistency from 2% to 16% led to a significant reduction in glucan conversion. However, the decrease ratio of glucan-glucose conversion was the minimum when the consistency increased from 2% to 12%. When the pretreated SSB consistency of 12% was applied for hydrolysis, increase in cellulase loading from 7.5 up to 20 filter paper units (FPU)/g glucan resulted only in 14% increase in glucan-glucose conversion compared to 20% increase with cellulase loading varying from 2.5 to 7.5 FPU/g glucan. More than 10 cellobiase units (CBU)/g glucan β-glucosidase supplementation had no noticeable improvement on glucan-glucose conversion. Additionally, supplementation of xylanase was found to significantly increase glucan-glucose conversion from 50% to 80% with the substrate consistency of 12%, when the cellulase and β-glucosidase loadings were at relatively low enzyme loadings (7.5 FPU/g and 10 CBU/g glucan). It appeared that residual xylan played a critical role in hindering the ease of hydrolysis of SSB. A proper xylanase addition was suggested to achieve a high hydrolysis yield at relatively high substrate consistency with relatively low enzyme loadings.

Details

Language :
English
ISSN :
1559-0291
Volume :
165
Issue :
3-4
Database :
MEDLINE
Journal :
Applied biochemistry and biotechnology
Publication Type :
Academic Journal
Accession number :
21728025
Full Text :
https://doi.org/10.1007/s12010-011-9317-9