• Applied Biological Chemistry
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• v.29 no.3
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• pp.266-272
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• 1986

The contents of water soluble ${\beta}-glucan$ were $1.4{\sim}4.0%$ in grains of 4 recommended varieties, and $0.3{\sim}0.6%$ in their malt. The ${\beta}-glucan$ content was subject to environmental factors such as cultivating region and nitrogen fertilizer level. The ${\beta}-glucan$ content of grains was positively correlated with the viscosity, but negatively with the protein and total gum contents. The ${\beta}-glucanase$ activity was $11.0{\sim}20.0$ sec as the reduced flow time in malt of 4 recommended varieties and was also subject to environmental factors. ${\beta}-Glucanase$ activity showed the highest level after the 6th day during malting. The ${\beta}-glucanase$ activity in malt was positively correlated with malt extract, but negatively with the residual ${\beta}-glucan$ content. The protein content in malt was negatively correlated with malt extract, but positively with the diastatic power.

• Journal of environmental and Sanitary engineering
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• v.10 no.2
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• pp.74-78
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• 1995

Several reports have suggested that these hydrolases( chitlnase, glucanase ) are likely volved in defense reactions in this Plant. In this paper, Induction by ethylene, mechanism, properties and function for Activation of these enzymes were Summarized.

• Journal of Microbiology and Biotechnology
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• v.26 no.5
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• pp.946-952
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• 2016

The eglS gene in Bacillus amyloliquefaciens encodes an endo-β-1,4-glucanase that belongs to glycosyl hydrolase family 5. In this study, a disruption mutant of gene eglS was constructed to examine its role in bacterial adaptation in plants. The mutant TB2_k, eglS gene inactivated bacterial strain, was remarkably impaired in extracellular cellulase activity. When inoculated on Brassica campestris, the TB2_k population was reduced by more than 60% compared with the wild-type strain in the root, stem, and leaf tissues. Overexpression of eglS in the wild-type strain increased the bacteria population in the plant tissues. Further studies revealed that the transcription level of eglS was correlated with bacterial population. These data demonstrate that endo-β-1,4-glucanase of B. amyloliquefaciens is required for its optimal endophytic colonization.

• Journal of Microbiology and Biotechnology
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• v.19 no.8
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• pp.818-822
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• 2009

A ${\beta}-1$,3-1,4-glucanase from the fungus Laetiporus sulphureus var. miniatus was purified as a single 26 kDa band by ammonium sulfate precipitation, HiTrap Q HP, and UNO Q ion-exchange chromatography, with a specific activity of 29 U/mg. The molecular mass of the native enzyme was 52 kDa as a dimer by gel filtration. ${\beta}-1$,3-1,4-Glucanase showed optimum activity at pH 4.0 and $75^{\circ}C$. The half-lives of the enzyme at $70^{\circ}C$ and $75^{\circ}C$ were 152 h and 22 h, respectively. The enzyme showed the highest activity for barley ${\beta}$-glucan as ${\beta}-1$,3-1,4-glucan among the tested polysaccharides and p-nitrophenyl-${\beta}$-D-glycosides with a $K_m$, of 0.67 mg/ml, a $k_{cat}$ of 13.5 $S^{-1}$ and a $k_{cat}/K_m$ of 20 mg/ml/s.

• Journal of Microbiology and Biotechnology
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• v.5 no.1
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• pp.26-30
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• 1995

The cytoplasmic endo-$\beta$-l, 4-glucanase (endoglucanase) was purified from cell extracts of Escherichia coli (pBS1) transformant carrying the Bacillus subtilis endo-$\beta$-l, 4-glucanase gene after full growth, and its molecular weight was found to be 52 kilodaltons (kDa). The endo-$\beta$-l, 4-glucanase isolated from the periplasmic space was smaller than 52-kDa cytoplasmic enzyme. The 52-kDa endoglucanase was found to be cleaved in the periplasm and finally converted to 34.5-kDa protein. Small amounts of both 52-kDa and 34.5-kDa proteins were secreted into the culture broth. The cleavage took place in the C-terminal portion of the enzyme. The N-terminal amino acid residues of both 52-kDa and 34.5-kDa enzymes were determined to be the same, Ala, the 30th residue of the primary translation product. Cleavage of the C-terminal portion showed to have no significant effect on the basic enzyme properties.

• Korean Journal of Agricultural Science
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• v.39 no.3
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• pp.387-393
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• 2012

In the present study, ${\beta}$-glucanase-assisted extraction of starch from glutinous barley(Hinchal ssalbory) was investigated. ${\beta}$-glucanase was added to a coarse starch suspension obtained after wet milling in the starch extraction process. It was found that in the isolated starch with enzyme treatment, protein content was lower by 0.03%, compared to that with non-enzyme treatment. More importantly it was observed that the extraction yield of starch from enzyme treatment was found to be about 12% higher than the one from non-enzyme treatment (enzyme treated: 90.56%, non-enzyme treated: 78.46%). In order to elucidate this finding, the mass-balance determination of starch in each extraction step was carried out and found that the enzyme treatment might influence on the insoluble residues(R3 and R4 fractions) to hydrolyze ${\beta}$-glucan and other materials (e.g., mucilages etc.), thereby facilitated the separation of starch from it and a next filtration process. With a phase-contrast microscope it was observed that the isolated starch with enzyme treatment contained small starch granules more than the one with non-enzyme treatment and this might result in higher extraction yield observed with the former. In order to confirm this hypothesis, further experiments would be necessary.

• KSBB Journal
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• v.19 no.4
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• pp.288-290
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• 2004

The cell wall of fifteen yeast strains were treated with Glucanex$^{(R)}$ 200G that contained mainly ${\beta}$1,3-glucanase and some ${\beta}$1,6-glucanase. In our previous study it was found that the yeasts that are more resistant to Glucanex$^{(R)}$ 200G treatment contained more ${\beta}$-glucan than the yeasts that are less resistant to Glucanex$^{(R)}$200G treatment. By measuring the resistance of cell wall to Glucanex$^{(R)}$ 200G, the relative content of ${\beta}$-glucan in yeast cell wall could be estimated. The resistance of cell wall to Glucanex$^{(R)}$ 200G was measured by counting viable cell number after reaction with and without Glucanex$^{(R)}$200G. The resistance of fifteen yeast strains to Glucanex$^{(R)}$ 200G were presented.ere presented.

• Korean Journal of Microbiology
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• v.44 no.1
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• pp.69-73
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• 2008

Fermented soybeans contain microorganisms, diverse enzymes, and bioactive compounds. Few studies on cellulase in Chungkookjang exist. Oligosaccharides play diverse roles of bioactivity. Through Congo red test and activity staining, it was confirmed that the enzyme solution contained cellulase. Optimal pH and temperature of the cellulase produced by Bacillus licheniformis B1 were 10 and $40^{\circ}C$, respectively. Through TLC analysis, it was demonstrated that the enzyme solution degraded carboxymethyl cellulose (CMC), whose main products contained dimer and trimer oligosaccharides. Cellulase activity of barley-Chungkookjnag fermented by the strain increased, compared with that of Chungkookjang. The cellulase was found to be a ${\beta}$-1,4-glucanase through the analysis of the cloned gene, showing polymorphism at 32 amino acid sites in the coding range of amino acid 10 and 460.

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.467-473
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• 2010

To improve the expression efficiency of recombinant endo-$\beta$-1,4-glucanase in P. pastoris, the endo-$\beta$-1,4-glucanase (egI) gene from Aspergillus niger was synthesized using optimized codons. Fourteen pairs of oligonucleotides with 15 bp overlap were designed and the full-length syn-egI gene was generated by two-step PCR-based DNA synthesis. In the synthesized endo-$\beta$-1,4-glucanase gene syn-egI, 193 nucleotides were changed, and the G+C content was decreased from 54% to 44.2%. The syn-egI gene was inserted into pPIC9K and transformed into P. pastoris GS115 by electroporation. The enzyme activity of recombinant P. pastoris stain 2-7# reached 20.3 U/ml with 1% barley $\beta$-glucan and 3.3 U/ml with 1% carboxymethylcellulose (CMC) as substrates in shake flasks versus 1,270.3 U/ml and 220.7 U/ml for the same substrates in 50-1 fermentors. The molecular mass of the recombinant protein was approximately 40 kDa as determined by SDS-PAGE analysis, the optimal temperature for recombinant enzyme activity was $70^{\circ}C$, and the optimal pH was 5.0 when CMC was used as the substrate.

• Korean Journal of Organic Agriculture
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• v.9 no.2
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• pp.55-67
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• 2001

Exogenous enzymes which, for the purpose of this paper, include phytase, $\beta$-glucanase, pentosanase and $\alpha$-galactosidase, are now extensively used throughout the world as aditives in swine diets. The chemical effects of these enzymes are well understand. However, the manner in which their benefits to the swine are brought about is still under debate. Phytase was to increase the availability of plant phytate phosphorus, which reduces phosphorus pollution and allows reductions in the amount of inorganic phosphate used. Also, enzymes have been discovered which have the potential to break down deleterious compounds commonly found in swine rations such as $\beta$-glucanase contained in barley and oats and the soluble pentosans found in rye and wheat thus increasing the digestibility of these non-starch polysaccharides. Future research in these area will allow for more efficient use of the current enzymes, development of more efficient future products and development of more thermotolerant enzymes.