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A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation

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Abstract

This review examines the recent models describing the mode of action of various xylanolytic enzymes and how these enzymes can be applied (sequentially or simultaneously) with their distinctive roles in mind to achieve efficient xylan degradation. With respect to homeosynergy, synergism appears to be as a result of β-xylanase and/or oligosaccharide reducing-end β-xylanase liberating xylo-oligomers (XOS) that are preferred substrates of the processive β-xylosidase. With regards to hetero-synergism, two cross relationships appear to exist and seem to be the reason for synergism between the enzymes during xylan degradation. These cross relations are the debranching enzymes such as α-glucuronidase or side-chain cleaving enzymes such as carbohydrate esterases (CE) removing decorations that would have hindered back-bone-cleaving enzymes, while backbone-cleaving-enzymes liberate XOS that are preferred substrates of the debranching and side-chain-cleaving enzymes. This interaction is demonstrated by high yields in co-production of xylan substituents such as arabinose, glucuronic acid and ferulic acid, and XOS. Finally, lytic polysaccharide monooxygenases (LPMO) have also been implicated in boosting whole lignocellulosic biomass or insoluble xylan degradation by glycoside hydrolases (GH) by possibly disrupting entangled xylan residues. Since it has been observed that the same enzyme (same Enzyme Commission, EC, classification) from different GH or CE and/or AA families can display different synergistic interactions with other enzymes due to different substrate specificities and properties, in this review, we propose an approach of enzyme selection (and mode of application thereof) during xylan degradation, as this can improve the economic viability of the degradation of xylan for producing precursors of value added products.

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Abbreviations

AA:

Auxiliary activity

Abf:

α-Arabinofuranosidase

Agu:

α-Glucuronidase

AGX:

Arabinoglucuronoxylan

AX:

Arabinoxylan

AXE:

Acetyl xylan esterase

AXH-d:

Doubly substituted L-Araf specific α-arabinofuranosidase

AXH-m:

Mono-substituted L-Araf specific α-arabinofuranosidase

CAZy:

Carbohydrate active enzyme database

CAZyme:

Carbohydrate-active enzyme

CE:

Carbohydrate esterase

DS:

Degree of synergy

EC:

Enzyme commission number

FA:

Ferulic acid

FAE:

Feruloyl esterase

GE:

Glucuronoyl esterase

GH:

Glycoside hydrolase

GX:

Glucuronoxylan

LPMO:

Lytic polysaccharide mono-oxygenase

Rex:

Oligosaccharide reducing-end xylanase

RS:

Reducing sugar(s)

XOS:

Xylo-oligosaccharide(s)

Xyn:

β-Xylanase

Xyl:

β-Xylosidase

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Authors and Affiliations

  1. Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, Eastern Cape, 6140, South Africa

    Samkelo Malgas, Mpho S. Mafa, Lithalethu Mkabayi & Brett I. Pletschke

  2. Protein Structure-Function Research Unit (PSFRU), School of Molecular and Cell Biology, Wits University, Johannesburg, Gauteng, 2000, South Africa

    Mpho S. Mafa

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  1. Samkelo Malgas
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  2. Mpho S. Mafa
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  3. Lithalethu Mkabayi
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  4. Brett I. Pletschke
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Correspondence to Brett I. Pletschke.

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The authors report no further conflicts of interest. The authors are responsible for the content and writing of this article and are grateful for financial support from the National Research Foundation (NRF) and Council for Scientific and Industrial Research (CSIR) in South Africa. Any opinion, findings and conclusions or recommendations expressed in this material are those of the author(s) and therefore the NRF does not accept any liability in regard thereto.

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Malgas, S., Mafa, M.S., Mkabayi, L. et al. A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation. World J Microbiol Biotechnol 35, 187 (2019). https://doi.org/10.1007/s11274-019-2765-z

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