Unraveling synergism between various GH family xylanases and deb ranching enzymes during hetero-xylan degradation

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dc.contributor.authorMalgas, Samkelo
dc.contributor.authorMafa, Mpho S.
dc.contributor.authorMathibe, Brian N.
dc.contributor.authorPletscke, Brett I.
dc.date.accessioned2022-08-19T07:46:51Z
dc.date.available2022-08-19T07:46:51Z
dc.date.issued2021
dc.description.abstractEnzymes classified with the same Enzyme Commission (EC) that are allotted in different glycoside hydrolase (GH) families can display different mechanisms of action and substrate specificities. Therefore, the combination of different enzyme classes may not yield synergism during biomass hydrolysis, as the GH family allocation of the enzymes influences their behavior. As a result, it is important to understand which GH family combinations are compatible to gain knowledge on how to efficiently depolymerize biomass into fermentable sugars. We evaluated GH10 (Xyn10D and XT6) and GH11 (XynA and Xyn2A) β-xylanase performance alone and in combination with various GH family α-l-arabinofuranosidases (GH43 AXH-d and GH51 Abf51A) and α-d-glucuronidases (GH4 Agu4B and GH67 AguA) during xylan depolymerization. No synergistic enhancement in reducing sugar, xylose and glucuronic acid released from beechwood xylan was observed when xylanases were supplemented with either one of the glucuronidases, except between Xyn2A and AguA (1.1-fold reducing sugar increase). However, overall sugar release was significantly improved (≥1.1-fold reducing sugar increase) when xylanases were supplemented with either one of the arabinofuranosidases during wheat arabinoxylan degradation. Synergism appeared to result from the xylanases liberating xylo-oligomers, which are the preferred substrates of the terminal arabinofuranosyl-substituent debranching enzyme, Abf51A, allowing the exolytic β-xylosidase, SXA, to have access to the generated unbranched xylo-oligomers. Here, it was shown that arabinofuranosidases are key enzymes in the efficient saccharification of hetero-xylan into xylose. This study demonstrated that consideration of GH family affiliations of the carbohydrate-active enzymes (CAZymes) used to formulate synergistic enzyme cocktails is crucial for achieving efficient biomass saccharification.en_ZA
dc.description.versionPublisher's versionen_ZA
dc.identifierhttps://doi.org/10.3390/molecules26226770
dc.identifier.citationMalgas, S., Mafa, M.S., Mathibe, B.N., & Platschte, B.I. (2021). Unraveling synergism between various GH family xylanases and deb ranching enzymes during hetero-xylan degradation. Molecules, 26, 6770. https://doi.org/10.3390/molecules26226770en_ZA
dc.identifier.issn1420-3049
dc.identifier.urihttp://hdl.handle.net/11660/11839
dc.language.isoenen_ZA
dc.publisherMDPIen_ZA
dc.rights.holderAuthor(s)en_ZA
dc.rights.licensehttps://creativecommons.org/licenses/by/4.0/
dc.subjectα-l-arabinofuranosidaseen_ZA
dc.subjectα-d-glucuronidaseen_ZA
dc.subjectβ-xylanaseen_ZA
dc.subjectGlycoside hydrolaseen_ZA
dc.subjectHeterosynergyen_ZA
dc.subjectXylan degradationen_ZA
dc.titleUnraveling synergism between various GH family xylanases and deb ranching enzymes during hetero-xylan degradationen_ZA
dc.typeArticleen_ZA
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