Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood

Várnai, Anikó; Huikko, Laura; Pere, Jaakko; Siika‐aho, Matti; Viikari, Liisa

doi:10.1016/j.biortech.2011.06.059

Cited by 143 publications

(98 citation statements)

References 30 publications

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“…TrCel7B was shown to be the most efficient single enzyme component in this process (Kont et al 2013). The relative efficiency of TrCel12A and TrCel7B in degrading of XOS and GOS is apparently due to their inherent hemicellulase activity (Biely et al 1991;Karlsson et al 2002;Varnai et al 2011).…”

Section: Discussionmentioning

confidence: 99%

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

Pellegrini

Serpa

Godoy

et al. 2015

Appl Microbiol Biotechnol

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Trichoderma filamentous fungi have been investigated due to their ability to secrete cellulases which find various biotechnological applications such as biomass hydrolysis and cellulosic ethanol production. Previous studies demonstrated that Trichoderma harzianum IOC-3844 has a high degree of cellulolytic activity and potential for biomass hydrolysis. However, enzymatic, biochemical, and structural studies of cellulases from T. harzianum are scarce. This work reports biochemical characterization of the recombinant endoglucanase I from T. harzianum, ThCel7B, and its catalytic core domain. The constructs display optimum activity at 55 °C and a surprisingly acidic pH optimum of 3.0. The full-length enzyme is able to hydrolyze a variety of substrates, with high specific activity: 75 U/mg for β-glucan, 46 U/mg toward xyloglucan, 39 U/mg for lichenan, 26 U/mg for carboxymethyl cellulose, 18 U/mg for 4-nitrophenyl β-D-cellobioside, 16 U/mg for rye arabinoxylan, and 12 U/mg toward xylan. The enzyme also hydrolyzed filter paper, phosphoric acid swollen cellulose, Sigmacell 20, Avicel PH-101, and cellulose, albeit with lower efficiency. The ThCel7B catalytic domain displays similar substrate diversity. Fluorescence-based thermal shift assays showed that thermal stability is highest at pH 5.0. We determined kinetic parameters and analyzed a pattern of oligosaccharide substrates hydrolysis, revealing cellobiose as a final product of C6 degradation. Finally, we visualized effects of ThCel7B on oat spelt using scanning electron microscopy, demonstrating the morphological changes of the substrate during the hydrolysis. The acidic behavior of ThCel7B and its considerable thermostability hold a promise of its industrial applications and other biotechnological uses under extremely acidic conditions.

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Section: Discussionmentioning

confidence: 99%

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

Pellegrini

Serpa

Godoy

et al. 2015

Appl Microbiol Biotechnol

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show abstract

“…It has been shown that different hemicellulases, e.g. xylanases and mannanases act in synergy in the decomposition [35]. Also in hemicellulose degradation, CBMs carried by these enzymes play a role, and either enhance the action of the hemicellulases or reduce non-productive binding onto lignin [36,37].…”

Section: Lignocellulose Its Carbohydrate Components and Carbohydratementioning

confidence: 99%

Thermostable Glycoside Hydrolases in Biorefinery Technologies

Linares-Pastén¹,

Andersson²,

Karlsson

2014

CBIOT

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Glycoside hydrolases, which are responsible for the degradation of the major fraction of biomass, the polymeric carbohydrates in starch and lignocellulose, are predicted to gain increasing roles as catalysts in biorefining applications in the future bioeconomy. In this context, thermostable variants will be important, as the recalcitrance of these biomass-components to degradation often motivates thermal treatments. The traditional focus on degradation is also predicted to be changed into more versatile roles of the enzymes, also involving specific conversions to defined products. In addition, integration of genes encoding interesting target activities opens the possibilities for whole cell applications, in organisms allowing processing at elevated temperatures for production of defined metabolic products.In this review, we overview the application of glycoside hydrolases related to the biorefining context (for production of food, chemicals, and fuels). Use of thermostable enzymes in processing of biomass is highlighted, moving from the activities required to act on different types of polymers, to specific examples in today's processing. Examples given involve (i) monosaccharide production for food applications as well as use as carbon source for microbial conversions (to metabolites such as fuels and chemical intermediates), (ii) oligosaccharide production for prebiotics applications (iii) treatment for plant metabolite product release, and (iv) production of surfactants of the alkyl glycoside class. Finally future possibilities in whole cell biorefining are shown.

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“…This review examines the enzymatic hydrolysis of mannan-based hemicellulose and the synergistic actions of mannanolytic enzymes required to achieve complete hydrolysis. This knowledge can improve bioconversion of mannan-containing lignocellulose substrates, leading to improved biofuel production; as the presence of hemicellulose (mannan) in lignocellulosic biomass is thought to act as a barrier to cellulose fibrils limiting access of cellulases to their substrate and thus cellulose hydrolysis (Banerjee et al 2010;Várnai et al 2011). …”

Section: Introductionmentioning

confidence: 99%

A review of the enzymatic hydrolysis of mannans and synergistic interactions between β-mannanase, β-mannosidase and α-galactosidase

Malgas

Dyk

Pletschke

2015

World J Microbiol Biotechnol

129

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Mannan is an important polysaccharide found in softwoods and many other plant sources. Mannans from various sources display large differences in composition, structure and complexity. To hydrolyse mannan into its monomer sugars requires a number of enzymes working in synergy. This review examines mannan structure and the enzymes required for its hydrolysis. Several studies have investigated the effect of supplementing β-mannanases with β-mannosidases and α-galactosidases in binary and ternary combinations. Synergistic enhancement of hydrolysis has been found in some, but not all cases. In the case of mannosidases, they sometimes display an anti-synergistic effect with mannanases, most likely due to competition for binding sites. Most importantly, in the case of α-galactosidases, the same enzyme from different families display differences in synergistic interactions due to different specificities. An improved understanding of enzyme interactions will aid in achieving enhanced hydrolysis of mannans and higher sugar yields. This review highlights areas which require further research in order to gain a better understanding of mannan hydrolysis and utilisation. Such knowledge is very important as this can be used in the optimisation of commercial or purified enzyme mixtures to improve the economic viability of the conversion of high mannan-containing biomass such as softwoods into fermentable sugars for bioethanol production.

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Synergistic action of xylanase and mannanase improves the total hydrolysis of softwood

Cited by 143 publications

References 30 publications

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme

Thermostable Glycoside Hydrolases in Biorefinery Technologies

A review of the enzymatic hydrolysis of mannans and synergistic interactions between β-mannanase, β-mannosidase and α-galactosidase

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