the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It is responsible for precisely hydrolyzing beta-1,4-glycosidic bonds adjacent to the beta-1,3-linkages in lichenan or mixed-linked beta-D-glucans, yielding mainly cellotriose, cellotetraose and cellopentaose
overexpression of barley (1->3,1->4)-beta-glucanase isoenzyme EII under the control of a promoter of barley D-Hordein gene Hor3-1 in barley cultivar Golden Promise. The T2 generation of transgenic lines shows increased activity of glucanase in grains. Total beta-glucan content is reduced by more than 95.73% in transgenic grains compared with the wild-type control. Overexpression leads to an increase in 1000-grain weight, which might be due to elevated amounts of starch in the grain
Streptomyces lydicus A01 expressing the enzyme shows substantially high glucanase activity, and has similar natamycin production and chitinase activity as the wild-type strain A01. Compared to the wild-type strain A01, the antifungal effects of Streptomyces lydicus AG01 on Botrytis cinerea, including inhibition of spore germination and mycelial growth, are highly improved. This is likely attributed to the heterologous expression of glucanase, which acts synergistically with natamycin and chitinase to increase the antifungal activity of the strain
endo-beta-1,3-1,4-glucanases are glycoside hydrolases involved in the enzymatic depolymerization of 1,3-1,4-beta-glucans and show antifungal activity against some fungi. Bacillus amyloliquefaciens BLB369 has a high antagonistic activity against phytopathogenic fungi. The purified recombinant enzyme has the ability to inhibit the growth of the phytopathogenic fungus Alternaria alternata
endo-beta-1,3-1,4-glucanases are glycoside hydrolases involved in the enzymatic depolymerization of 1,3-1,4-beta-glucans and show antifungal activity against some fungi. Bacillus amyloliquefaciens BLB369 has a high antagonistic activity against phytopathogenic fungi. The purified recombinant enzyme has the ability to inhibit the growth of the phytopathogenic fungus Alternaria alternata
Streptomyces lydicus A01 expressing the enzyme shows substantially high glucanase activity, and has similar natamycin production and chitinase activity as the wild-type strain A01. Compared to the wild-type strain A01, the antifungal effects of Streptomyces lydicus AG01 on Botrytis cinerea, including inhibition of spore germination and mycelial growth, are highly improved. This is likely attributed to the heterologous expression of glucanase, which acts synergistically with natamycin and chitinase to increase the antifungal activity of the strain
both the loss of the signal peptide (29 amino acids) and the addition of the His-tag to the peptide backbone do not affect the specific activity of linear enzyme
Glu56, Asp58 and Glu60 residues located in the active site cavity of the enzyme play key roles in enzyme catalysis, functioning as general acid-base residues, structure and functional relationships of Fsbeta-glucanase
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview