• Applied Biological Chemistry
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• v.42 no.4
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• pp.324-329
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• 1999

Barley malts were prepared at 15, 18 and $21^{\circ}C$ for $3{\sim}6$ days, and assayed for ${\beta}-glucanase$, ${\alpha}-amylase$ and ${\beta}-amylase$ activities. ${\beta}-Glucanase$ activity increased markedly during earley germination and reached maximum at the 6th day of germination. ${\beta}-Glucanase$ activity in six-rowed barley malt was much higher than that in two-rowed malt. ${\beta}-Glucanase$ activity was associated with reduction in ${\beta}-glucan$ content during germination. ${\beta}-amylase$ activity was also considerably higher in two-rowed barley, and increased continuously during 6-day germination. ${\beta}-Amylase$ activity was the lowest at $15^{\circ}C$, the highest at $18^{\circ}C$, and intermediate at $21^{\circ}C$ of germination temperature. Considerable amount of ${\beta}-amylase$ was detected in ungerminated raw barley, and this enzymatic activity tended to increase during 6-day germination. Diastatic power, measure of starch-saccharifying enzyme, in six-rowed malt was $1.4{\sim}1.6$ fold higher than in two-rowed malt. Germination at $18^{\circ}C$ for $5{\sim}6$ days was suggested to be the optimum condition for manufacturing good quality malts, in terms of enhanced starch-degrading enzymatic activity.

• Asian-Australasian Journal of Animal Sciences
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• v.9 no.3
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• pp.303-307
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• 1996

The degree of autolysis and presence of cell-wall degrading enzymes in an anaerobic ruminal fungus, Piromyces communis OTSI, grown in liquid medium, was monitored to evaluate the effect of self-digestion on fungal biomass. After a 30 days incubation period fungal dry weight decreased by 45% and the cell wall component chitin decreased by 22%. Chitinase activity detected in the supernatant was mainly of the endotype and peaked at day 6 of the incubation. ${\beta}-1$, 3-glucanase was detected from day 4 and increased throughout the incubation period. Autolysis was a slow process, and under natural conditions it is unlikely that it plays a significant role in the degradation of the spent fungal vegetative stage in the rumen.

• Korean Journal of Microbiology
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• v.37 no.4
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• pp.253-258
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• 2001

A Bacillus circulans KCTC3004 $\beta$-1,3-glucanase gene contained in a recombinant plasmid pLM460 derived from subcloning the original recombinant plasmid pLM530 was trasferred into a new shuttle vector plasmid pLMS1180 by ligating linearized DNAs of pLM460 and pUB110. B. subtilis RM125 and B. megaterium ATCC14945 transformed with pLMS1180 produced the $\beta$-1,3-glucanase substantially. Most of the enzyme was produced during the exponential growth period. The maxium activities of the $\beta$-1,3-glucanase produced by the Bacillus transformants were compared with that of the B. circulans gene donor strain. The B. subtilis RM125 (pLM1180) enzyme showed the activity 14 times higher than that of the gene donor cells, followed by the B. megaterium ATCC14945 (pLMS 1180) enzyme with activity 5 times higher than that of the gene donor cells. While E. coli secreted about 7% of the produced enzyme, B. subtilis excreted the enzyme into the medium wholly and B. megaterium about 97% of the total product. The SDS-PAGE of this enzyme produced in E. coli (pLMS1180), B subtilis (pLMS1180) or B. megaterium (pLMS1180) indicated a molecular weight of 38,000. The enzymes overproduced in three different host cells hydrolyzed laminarin to produce mainly laminaribiose, laminaritriose, and laminarioligosaccharides. The plasmid pLMS1180 was stable in B. megaterium, E. coli, but was unstable in B. subtilis.

• Applied Biological Chemistry
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• v.37 no.1
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• pp.43-48
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• 1994

A basic inducible protein, ICG, containing chitinase and ${\beta}-1,3-glucanase$ activity concomittantly was purified from cell suspension culture media of rice after the treatment of chitooligosaccharides. The isolated ICG enzyme gave a single band on native and SDS polyacrylamide gel electrophoresis and its molecular weight was estimated to be 52.53 kd. The optimal temperature and optimal pH of both enzyme activities in ICG were $60^{\circ}C$, pH 6.0 for chitinase activity and $37^{\circ}C$, pH 4.0 for ${\beta}-1,3-glucanase$ activity. $K_M$ and $V_{max}$ values for chitinase were 0.474 mM. 2.997 nM/min., and those for ${\beta}-1,3-glucanase$ were 1.004 mM 0.739 nM/min. respectively. TLC analysis of the chitooligosaccharide hydrolysates with ICG enzyme indicated that ICG acts as endochitinase.

• Journal of Life Science
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• v.13 no.3
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• pp.355-358
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• 2003

Various Trichoderma spp. were evaluated for the development of biofungicides to control soilborne pathogen, Rhiztonia solani, Various Trichoderma spp. were initially tested for their ability to inhibit growth of R. solani by inhibition zone test. Inhibition zones of 3∼5 mm toward R. solani were detected on PDA agar plates. The parasitic activity of strains, the activities of cell-wall-degrading enzymes such as glucanases and chitinases, were also evaluated. Highest activities of glucanase and chitinase were 3.5 U/ml and 0.9 U/ml, respectively, Isolated Trichoderma spp. also exhibited good growth with currently used agrochemicals, which represents that the isolated biofungicides can be mutually used with agrochemicals.

• Korean Journal of Microbiology
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• v.24 no.3
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• pp.295-301
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• 1986

The bacteria, which were capable of producing ${\beta}-1$, 3-glucanase inducibly by utilizing cell wall of Aspergillus fumigatus as a sole carbon source, were isolated from soil in the campus of Kyungpook National University. Among them, the strain which produced the enzyme excellently was selected and identified to be Pseudomonas stutzeri KF 13 by morphological, cultural and physiological examination. The optimal conditions for the enzyme production from Pseudomonas stutzeri KF 13 were investigated. the enzyme production was reached maximum state shen the broth cultured for 72hr at $30^{\circ}C$. And the enzyme showed the highest activity in the medium containing 3.5% cell wall as an inducer, 15% yeast autolysate as a nitrogen source and 0.05% $MnSO_4$ at pH 7.5.

• Korean Journal of Microbiology
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• v.25 no.1
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• pp.1-8
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• 1987

An extracellular $\beta$-1, 3-glucanase from Pseudomonas stutzeri KF 13 was purified about 390 with 26% recovery. The purified enzyme revealed a single band by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The enzyme was stable in a pH 6.0 to 9.0, and relatively thermostable. The optimal pH and temperature on the enzyme activity were found to be 5.8 and 45.deg.C, respectively. The activation energy was calculated to be 16,130 cal per mole. The Km value for laminarin was found to be 3ng per ml and the molecular weight was determined to be 28,000 by gel filtration and 26,000 daltons by SDS-acrylamide gel electrophoresis. The enzyme was inhibited by 1.0mM of $Hg^{2+}$, and strongly inhibited by 1.0mM of p-chloromercuribenzoic acid.

• Korean Journal of Microbiology
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• v.26 no.3
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• pp.223-229
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• 1988

Bacillus subtilis K-4-3, which produces considerable amount of $\beta$-glucanase was selected among extracellular $\beta$-glucanase-producing bacteria isolated from soil. $\beta$-glucanase was purified by ammonium sulfate fractionation, Sephadex G-100 gel filtration and DEAE-sephacel ion exchange chromatography. The purified enzyme revealed a single band by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 17000 dalton by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature of the purified $\beta$-glucanase were 7.0 and $50^{\circ}C$, respectively. The enzyme was strongly inhibited by 1.0mM of $Fe^{3+}$, and activated by 1.0mm of $Li^{}47+$. The absence of glucose after thin layer chromatography of reaction products revealed that the purified enzyme contains no cellobiase or laminarinbiase activity. The loberation of ki, tri-and tetra-saccharide as reaction products can be explained by endoaction of the enzyme.

• 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.

• Korean Journal of Microbiology
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• v.25 no.4
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• pp.339-345
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• 1987

A bacterium K-4-3, producing $\beta$-glucan hydrolyzing enzyme, was isolated from soil and identified to be Bacillus subtilis by its morpholohical and physiological characteristics. $\beta$-glucan was coloured using cibacron blue 3G-A and cross linded by the addition of 1, 4-butanedioldiglycidyl ether. This substrate was used for the isolation of $\beta$-glucanase producing microorganism. The $\beta$-glucan hydrolyzing enzyme actibity from isolated K-4-3 strain was also measured using the modified substrate. Bacillus subtilis K-4-3 produced the highest extracellular $\beta$-glucan hydrolyzing activity in the basal medium containing $\beta$-glucan as a carbon source, peptone and tryptone as a nitrogen source, and magnesium sulfate as an inorganic salt. The optimum temperature and initial pH for $\beta$-glucanase production by Bacillus subtilis K-4-3 were $37^{\circ}C$ and pH6. The highest enzyme activity was obtained at the culture age of 54 hrs with rotary shaking at $37^{\circ}C$. The crude enzyme showed the highest activity at pH 7.5-8.0 and $65^{\circ}C$.