Formulation of enzyme blends to maximize the hydrolysis of alkaline peroxide pretreated alfalfa hay and barley straw by rumen enzymes and commercial cellulases

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creativework.keywords - en
Rumen fermentation
Glycosidases
Enzymes
Hydrolysis
Esterases
creativework.keywords - fr
Glycosidases
Fermentation dans la panse
Enzymes
Hydrolyse
Estérases
dc.contributor.author
Badhan, Ajay
Wang, Yuxi
Gruninger, Robert
Patton, Donald
Powlowski, Justin
Tsang, Adrian
McAllister, Tim
dc.date.accepted
2014-04-16
dc.date.accessioned
2025-09-29T15:17:24Z
dc.date.available
2025-09-29T15:17:24Z
dc.date.issued
2014-04-26
dc.date.submitted
2014-01-30
dc.description.abstract - en
Background Efficient conversion of lignocellulosic biomass to fermentable sugars requires the synergistic action of multiple enzymes; consequently enzyme mixtures must be properly formulated for effective hydrolysis. The nature of an optimal enzyme blends depends on the type of pretreatment employed as well the characteristics of the substrate. In this study, statistical experimental design was used to develop mixtures of recombinant glycosyl hydrolases from thermophilic and anaerobic fungi that enhanced the digestion of alkaline peroxide treated alfalfa hay and barley straw by mixed rumen enzymes as well as commercial cellulases (Accelerase 1500, A1500; Accelerase XC, AXC). Results Combinations of feruloyl and acetyl xylan esterases (FAE1a; AXE16A_ASPNG), endoglucanase GH7 (EGL7A_THITE) and polygalacturonase (PGA28A_ASPNG) with rumen enzymes improved straw digestion. Inclusion of pectinase (PGA28A_ASPNG), endoxylanase (XYN11A_THITE), feruloyl esterase (FAE1a) and β-glucosidase (E-BGLUC) with A1500 or endoglucanase GH7 (EGL7A_THITE) and β-xylosidase (E-BXSRB) with AXC increased glucose release from alfalfa hay. Glucose yield from straw was improved when FAE1a and endoglucanase GH7 (EGL7A_THITE) were added to A1500, while FAE1a and AXE16A_ASPNG enhanced the activity of AXC on straw. Xylose release from alfalfa hay was augmented by supplementing A1500 with E-BGLUC, or AXC with EGL7A_THITE and XYN11A_THITE. Adding arabinofuranosidase (ABF54B_ASPNG) and esterases (AXE16A_ASPNG; AXE16B_ASPNG) to A1500, or FAE1a and AXE16A_ASPNG to AXC enhanced xylose release from barley straw, a response confirmed in a scaled up assay. Conclusion The efficacy of commercial enzyme mixtures as well as mixed enzymes from the rumen was improved through formulation with synergetic recombinant enzymes. This approach reliably identified supplemental enzymes that enhanced sugar release from alkaline pretreated alfalfa hay and barley straw.
dc.identifier.citation
Badhan, A., Wang, Y., Gruninger, R., Patton, D., Powlowski, J., Tsang, A., & McAllister, T. (2014). Formulation of enzyme blends to maximize the hydrolysis of alkaline peroxide pretreated alfalfa hay and barley straw by rumen enzymes and commercial cellulases. BMC Biotechnology, 14, Article 13. https://doi.org/10.1186/1472-6750-14-31
dc.identifier.doi
https://doi.org/10.1186/1472-6750-14-31
dc.identifier.issn
1472-6750
dc.identifier.uri
https://open-science.canada.ca/handle/123456789/3900
dc.language.iso
en
dc.publisher - en
BioMed Central Ltd.
dc.publisher - fr
BioMed Central Ltd.
dc.rights - en
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.rights - fr
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.rights.uri - en
https://creativecommons.org/licenses/by/4.0/
dc.rights.uri - fr
https://creativecommons.org/licenses/by/4.0/deed.fr
dc.subject - en
Animal nutrition
dc.subject - fr
Alimentation animale
dc.subject.en - en
Animal nutrition
dc.subject.fr - fr
Alimentation animale
dc.title - en
Formulation of enzyme blends to maximize the hydrolysis of alkaline peroxide pretreated alfalfa hay and barley straw by rumen enzymes and commercial cellulases
dc.type - en
Article
dc.type - fr
Article
local.acceptedmanuscript.articlenum
13
local.article.journaltitle - en
BMC Biotechnology
local.article.journalvolume
14
local.pagination
1-14
local.peerreview - en
Yes
local.peerreview - fr
Oui
local.requestdoi - en
No
local.requestdoi - fr
No
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