Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation

Enzymes 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, a...

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Autores principales:	Samkelo Malgas, Mpho S. Mafa, Brian N. Mathibe, Brett I. Pletschke
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	α-<span style="font-variant: small-caps">l</span>-arabinofuranosidase α-<span style="font-variant: small-caps">d</span>-glucuronidase β-xylanase glycoside hydrolase hetero-synergy xylan degradation Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/1950e8bb758a4a529c25da1f811a9368
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spelling	oai:doaj.org-article:1950e8bb758a4a529c25da1f811a93682021-11-25T18:27:07ZUnraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation10.3390/molecules262267701420-3049https://doaj.org/article/1950e8bb758a4a529c25da1f811a93682021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/22/6770https://doaj.org/toc/1420-3049Enzymes 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-<span style="font-variant: small-caps;">l</span>-arabinofuranosidases (GH43 AXH-d and GH51 Abf51A) and α-<span style="font-variant: small-caps;">d</span>-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 <i>xylo</i>-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 <i>xylo</i>-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.Samkelo MalgasMpho S. MafaBrian N. MathibeBrett I. PletschkeMDPI AGarticleα-<span style="font-variant: small-caps">l</span>-arabinofuranosidaseα-<span style="font-variant: small-caps">d</span>-glucuronidaseβ-xylanaseglycoside hydrolasehetero-synergyxylan degradationOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6770, p 6770 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	α-<span style="font-variant: small-caps">l</span>-arabinofuranosidase α-<span style="font-variant: small-caps">d</span>-glucuronidase β-xylanase glycoside hydrolase hetero-synergy xylan degradation Organic chemistry QD241-441
spellingShingle	α-<span style="font-variant: small-caps">l</span>-arabinofuranosidase α-<span style="font-variant: small-caps">d</span>-glucuronidase β-xylanase glycoside hydrolase hetero-synergy xylan degradation Organic chemistry QD241-441 Samkelo Malgas Mpho S. Mafa Brian N. Mathibe Brett I. Pletschke Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
description	Enzymes 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-<span style="font-variant: small-caps;">l</span>-arabinofuranosidases (GH43 AXH-d and GH51 Abf51A) and α-<span style="font-variant: small-caps;">d</span>-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 <i>xylo</i>-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 <i>xylo</i>-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.
format	article
author	Samkelo Malgas Mpho S. Mafa Brian N. Mathibe Brett I. Pletschke
author_facet	Samkelo Malgas Mpho S. Mafa Brian N. Mathibe Brett I. Pletschke
author_sort	Samkelo Malgas
title	Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
title_short	Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
title_full	Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
title_fullStr	Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
title_full_unstemmed	Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation
title_sort	unraveling synergism between various gh family xylanases and debranching enzymes during hetero-xylan degradation
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/1950e8bb758a4a529c25da1f811a9368
work_keys_str_mv	AT samkelomalgas unravelingsynergismbetweenvariousghfamilyxylanasesanddebranchingenzymesduringheteroxylandegradation AT mphosmafa unravelingsynergismbetweenvariousghfamilyxylanasesanddebranchingenzymesduringheteroxylandegradation AT briannmathibe unravelingsynergismbetweenvariousghfamilyxylanasesanddebranchingenzymesduringheteroxylandegradation AT brettipletschke unravelingsynergismbetweenvariousghfamilyxylanasesanddebranchingenzymesduringheteroxylandegradation
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Unraveling Synergism between Various GH Family Xylanases and Debranching Enzymes during Hetero-Xylan Degradation

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