Biochemical characterization of a 27kDa 1,3-β-d-glucanase from Trichoderma asperellum induced by cell wall of Rhizoctonia solani

Aires, Raquel da Silva; Steindorff, Andrei Stecca; Ramada, Marcelo Henrique Soller; Siqueira, Saulo José Linhares de; Ulhôa, Cirano José

doi:10.1016/j.carbpol.2011.09.001

Cited by 28 publications

(11 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The common broad specificity of ␤-1,3-glucanases is the cleavage action on ␤-1,3-1,4-glucans through the ␤-1,3-1,4-glucanase activity (37). However, this catalytic activity was not observed for Gly5M in this study.…”

Section: Discussioncontrasting

confidence: 60%

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity

Wang

Kim

Seo

et al. 2016

Appl Environ Microbiol

View full text Add to dashboard Cite

In this study, we characterized Gly5M, originating from a marine bacterium, as a novel ␤-1,3-1,6-endoglucanase in glycoside hydrolase family 5 (GH5) in the Carbohydrate-Active enZyme database. The gly5M gene encodes Gly5M, a newly characterized enzyme from GH5 subfamily 47 (GH5_47) in Saccharophagus degradans 2-40 T . The gly5M gene was cloned and overexpressed in Escherichia coli. Through analysis of the enzymatic reaction products by thin-layer chromatography, high-performance liquid chromatography, and matrix-assisted laser desorption ionization-tandem time of flight mass spectrometry, Gly5M was identified as a novel ␤-1,3-endoglucanase (EC 3.2.1.39) and bacterial ␤-1,6-glucanase (EC 3.2.1.75) in GH5. The ␤-1,3-endoglucanase and ␤-1,6-endoglucanase activities were detected by using laminarin (a ␤-1,3-glucan with ␤-1,6-glycosidic linkages derived from brown macroalgae) and pustulan (a ␤-1,6-glucan derived from fungal cell walls) as the substrates, respectively. This enzyme also showed transglycosylase activity toward ␤-1,3-oligosaccharides when laminarioligosaccharides were used as the substrates. Since laminarin is the major form of glucan storage in brown macroalgae, Gly5M could be used to produce glucose and laminarioligosaccharides, using brown macroalgae, for industrial purposes. IMPORTANCEIn this study, we have discovered a novel ␤-1,3-1,6-endoglucanase with a unique transglycosylase activity, namely, Gly5M, from a marine bacterium, Saccharophagus degradans 2-40 T . Gly5M was identified as the newly found ␤-1,3-endoglucanase and bacterial ␤-1,6-glucanase in GH5. Gly5M is capable of cleaving glycosidic linkages of both ␤-1,3-glucans and ␤-1,6-glucans. Gly5M also possesses a transglycosylase activity toward ␤-1,3-oligosacchrides. Due to the broad specificity of Gly5M, this enzyme can be used to produce glucose or high-value ␤-1,3-and/or ␤-1,6-oligosaccharides. Marine macroalgae have been considered as potential sources of carbohydrates for the production of biofuels and biologically based products (1). Among the marine macroalgae, over 70 million tons of brown macroalgae are produced annually (2). The major carbon storage compounds of brown algae are alginate, laminarin, fucoidan, and mannitol (3). Laminarin is a linear polysaccharide composed of D-glucose with ␤-1,3-glycosidic linkages in the main backbone and degrees of polymerization (DPs) of 20 to 25 (4), with some 6-O-branching from D-glucose in the main chain and some ␤-1,6-glycosidic linkages as branches; the ␤-1,3-glucan/␤-1,6-glucan ratio is approximately 3:1, depending on the species of brown macroalgae (5). Among brown macroalgae, the main sources of laminarin are Laminaria and Saccharina spp. For instance, Laminaria hyperborean and Saccharina latissima contain laminarin at up to 32% of dry weight (6), and 84% of total carbohydrates are laminarin in Fucus vesiculosus (7). Unlike other marine polysaccharides, such as alginate and agar, from which monomeric sugars are not fermentable by terrestrial microorganisms (8, 9), the final hydrolys...

show abstract

Section: Discussioncontrasting

confidence: 60%

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity

Wang

Kim

Seo

et al. 2016

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…2a), showing approximately 75% activity at 40∞C and 80∞C and less than 60% activity at a temperature above 90∞C. The optimal temperature of the enzyme was close to that previously reported from Bacillus sources, but lower than some thermophilic glucanases from thermophilic and ultra-thermophilic bacteria (Da Silva Aires et al, 2012;Kim et al, 2000;Koutsopoulos et al, 2005;Murray et al, 2001;Ueda et al, 2014). Thermostability assays (Fig.…”

Section: Characterization Of Recombinant Enzymesupporting

confidence: 84%

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Wei

Deng

et al. 2017

J. Gen. Appl. Microbiol.

View full text Add to dashboard Cite

show abstract

“…In the hydrolysis process the GH17 introduces short terminal β-1,6 branches on the glucan [ 27 ] and the GH72 elongates another β-glucan on the non-reducing end [ 30 ]. The endo-β-1,3(4)-glucanase from GH16 was shown to degrade mixed linkage β-glucan from barley by specifically hydrolyzing internal β-1,3 linkage [ 28 , 29 ]. There were also three endoglucanases (Cel5A, Cel7B, cel12A) and a β-glucosidase Cel3A in the T .…”

Section: Discussionmentioning

confidence: 99%

Multicomponent carbohydrase system from Trichoderma reesei: A toolbox to address complexity of cell walls of plant substrates in animal feed

Pedersen

Tovborg

Farjam³

et al. 2021

PLoS ONE

View full text Add to dashboard Cite

A diverse range of monocot and dicot grains and their by-products are commonly used in the animal feed industry. They all come with complex and variable cell wall structures which in turn contribute significant fiber to the complete feed. The cell wall is a highly interconnected matrix of various polysaccharides, proteins and lignin and, as such, requires a collaborative effort of different enzymes for its degradation. In this regard, we investigated the potential of a commercial multicomponent carbohydrase product from a wild type fermentation of Trichoderma reesei (T. reesei) (RONOZYME® MultiGrain) in degrading cell wall components of wheat, barley, rye, de-oiled rice bran, sunflower, rapeseed and cassava. A total of thirty-one different enzyme proteins were identified in the T. Reesei carbohydrase product using liquid chromatography with tandem mass spectrometry LC-MS/MS including glycosyl hydrolases and carbohydrate esterases. As measured by in vitro incubations and non-starch polysaccharide component analysis, and visualization by immunocytochemistry and confocal microscopy imaging of immuno-labeled samples with confocal microscopy, the carbohydrase product effectively solubilized cellulolytic and hemicellulolytic polysaccharides present in the cell walls of all the feed ingredients evaluated. The T. reesei fermentation also decreased viscosity of arabinoxylan, xyloglucan, galactomannan and β-glucan substrates. Combination of several debranching enzymes including arabinofuranosidase, xylosidase, α-galactosidase, acetyl xylan esterase, and 4-O-methyl-glucuronoyl methylesterase with both GH10 and GH11 xylanases in the carbohydrase product resulted in effective hydrolyzation of heavily branched glucuronoarabinoxylans. The different β-glucanases (both endo-β-1,3(4)-glucanase and endo-β-1,3-glucanase), cellulases and a β-glucosidase in the T. reesei fermentation effectively reduced polymerization of both β-glucans and cellulose polysaccharides of viscous cereals grains (wheat, barley, rye and oat). Interestingly, the secretome of T. reesei contained significant amounts of an exceptional direct chain-cutting enzyme from the GH74 family (Cel74A, xyloglucan-specific β-1,4-endoglucanase), that strictly cleaves the xyloglucan backbone at the substituted regions. Here, we demonstrated that the balance of enzymes present in the T. reesei secretome is capable of degrading various cell wall components in both monocot and dicot plant raw material used as animal feed.

show abstract

Biochemical characterization of a 27kDa 1,3-β-d-glucanase from Trichoderma asperellum induced by cell wall of Rhizoctonia solani

Cited by 28 publications

References 24 publications

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Multicomponent carbohydrase system from Trichoderma reesei: A toolbox to address complexity of cell walls of plant substrates in animal feed

Contact Info

Product

Resources

About

Biochemical characterization of a 27kDa 1,3-β-d-glucanase from Trichoderma asperellum induced by cell wall of Rhizoctonia solani

Cited by 28 publications

References 24 publications

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 T and Its Transglycosylase Activity

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 T and Its Transglycosylase Activity

Expression and biochemical characterization of a multifunctional glycosidase from the thermophilic <i>Bacillus licheniformis</i> SR01

Multicomponent carbohydrase system from Trichoderma reesei: A toolbox to address complexity of cell walls of plant substrates in animal feed

Contact Info

Product

Resources

About

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity

A Novel Glycoside Hydrolase Family 5 β-1,3-1,6-Endoglucanase from Saccharophagus degradans 2-40 ^T and Its Transglycosylase Activity