Cellulase and xylanase synergism in industrial biotechnology

Bajaj, Priyanka; Mahajan, Ritu

doi:10.1007/s00253-019-10146-0

Cited by 110 publications

(33 citation statements)

References 162 publications

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“…These metal salts and chemical reagents are commonly present in industrial practices and may have impacts on enzymatic activities (Boyce and Walsh, 2015;Wang et al, 2019). Thus, the cation and chemical resistance of CtCel7 is an evaluation index for its industrial applications, such as environmental waste treatment, functional oligosaccharide extraction and bioethanol production (Bajaj and Mahajan, 2019;Patel et al, 2019;Yang et al, 2019). The enzyme in the absence of metal ions or reagents was used as a control (Jeon et al, 2016).…”

Section: Effect Of Cations and Chemicals On Enzyme Activitymentioning

confidence: 99%

Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation

Han

Yang

Sun

et al. 2020

Front. Bioeng. Biotechnol.

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The novel cellobiohydrolase gene ctcel7 was identified from Chaetomium thermophilum, and its recombinant protein CtCel7, a member of glycoside hydrolase family 7, was heterologously expressed in Pichia pastoris and biochemically characterized. Compared with commercial hydrolases, purified CtCel7 exhibited superior bifunctional cellobiohydrolase and xylanase activities against microcrystalline cellulose and xylan, respectively, under optimal conditions of 60 • C and pH 4.0. Moreover, CtCel7 displayed remarkable thermostability with over 90% residual activity after heat (60 • C) treatment for 180 min. CtCel7 was insensitive to most detected cations and reagents and preferentially cleaved the β-1,4-glycosidic bond to generate oligosaccharides through the continuous saccharification of lignocellulosic substrates, which are crucial for various practical applications. Notably, the hydrolysis effect of a commercial cellulase cocktail on pretreated wheat straw was substantively improved by its combination with CtCel7. Taken together, these excellent properties distinguish CtCel7 as a robust candidate for the biotechnological production of biofuels and biobased chemicals.

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Section: Effect Of Cations and Chemicals On Enzyme Activitymentioning

confidence: 99%

Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation

Han

Yang

Sun

et al. 2020

Front. Bioeng. Biotechnol.

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“…The plate assay has been used for decades as a primary screening method to select xylanase producing strains. The screening strains are cultured on agar medium containing xylan as their carbon source until clear zones are observed (the xylan hydrolysis area) after being stained with Congo red dye [183] or Gram's iodine solution [184]. Plate assay methods rely on interactions between a dye and a polymeric substrate for the indirect detection of hydrolysis but require the use of relevant controls and independent confirmation of the relevant enzymatic activities.…”

Section: Hemicellulose Degradation Enzymesmentioning

confidence: 99%

“…Endo-xylanases randomly hydrolyze β-1,4-xylanopyranosyl linkages of xylan to form xylo-oligosaccharides, xylotriose, xylobiose and xylose. The hydrolysis of xylans is not attacked randomly but depends upon the degree of branching, chain length, and presence of substituents in the substrate molecule [ 183 ].…”

Section: Lignocellulolytic Enzyme Production By Mushroom Using Agrmentioning

confidence: 99%

Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste

et al. 2020

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A large amount of agro-industrial waste is produced worldwide in various agricultural sectors and by different food industries. The disposal and burning of this waste have created major global environmental problems. Agro-industrial waste mainly consists of cellulose, hemicellulose and lignin, all of which are collectively defined as lignocellulosic materials. This waste can serve as a suitable substrate in the solid-state fermentation process involving mushrooms. Mushrooms degrade lignocellulosic substrates through lignocellulosic enzyme production and utilize the degraded products to produce their fruiting bodies. Therefore, mushroom cultivation can be considered a prominent biotechnological process for the reduction and valorization of agro-industrial waste. Such waste is generated as a result of the eco-friendly conversion of low-value by-products into new resources that can be used to produce value-added products. Here, we have produced a brief review of the current findings through an overview of recently published literature. This overview has focused on the use of agro-industrial waste as a growth substrate for mushroom cultivation and lignocellulolytic enzyme production.

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“…Enzymatic degradation of xylan does not generate these harmful effects and is therefore of interest both in processes focusing on cellulose and more holistic ones targeting all cell wall carbohydrates. Indeed, in many industrial applications, cellulases and xylanases are used simultaneously in order to provide the greatest yields of usable sugars [13].…”

Section: Introductionmentioning

confidence: 99%

Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules

Krska

Larsbrink

2020

Biotechnol Biofuels

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Background: Efficient degradation of lignocellulosic biomass has become a major bottleneck in industrial processes which attempt to use biomass as a carbon source for the production of biofuels and materials. To make the most effective use of the source material, both the hemicellulosic as well as cellulosic parts of the biomass should be targeted, and as such both hemicellulases and cellulases are important enzymes in biorefinery processes. Using thermostable versions of these enzymes can also prove beneficial in biomass degradation, as they can be expected to act faster than mesophilic enzymes and the process can also be improved by lower viscosities at higher temperatures, as well as prevent the introduction of microbial contamination. Results: This study presents the investigation of the thermostable, dual-function xylanase-glucuronoyl esterase enzyme CkXyn10C-GE15A from the hyperthermophilic bacterium Caldicellulosiruptor kristjanssonii. Biochemical characterization of the enzyme was performed, including assays for establishing the melting points for the different protein domains, activity assays for the two catalytic domains, as well as binding assays for the multiple carbohydratebinding domains present in CkXyn10C-GE15A. Although the enzyme domains are naturally linked together, when added separately to biomass, the expected boosting of the xylanase action was not seen. This lack of intramolecular synergy might suggest, together with previous data, that increased xylose release is not the main beneficial trait given by glucuronoyl esterases. Conclusions: Due to its thermostability, CkXyn10C-GE15A is a promising candidate for industrial processes, with both catalytic domains exhibiting melting temperatures over 70 °C. Of particular interest is the glucuronoyl esterase domain, as it represents the first studied thermostable enzyme displaying this activity.

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Cellulase and xylanase synergism in industrial biotechnology

Cited by 110 publications

References 162 publications

Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation

Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation

Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste

Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme from Caldicellulosiruptor kristjanssonii incorporating multiple carbohydrate-binding modules

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