• KOREAN JOURNAL OF CROP SCIENCE
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• v.40 no.2
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• pp.250-254
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• 1995

Isolated barley aleurone layers were used to examine response of (1-3)- and $(1-3,1-4)-{\beta}-glucanases{\;}to{\;}GA_3$. Protein content and levels of (1-3)- and $(1-3,1-4)-{\beta}-glucanases$ increased in the presense of added $GA_3$. However, (1-3)- and $(1-3,1-4)-{\beta}-glucanases$ showed different response to $GA_3$ in their production and secretion patterns. $(1-3,1-4)-{\beta}-glucanases$ showed higher increase in enzyme activity than $(1-3)-{\beta}-glucanase$ in the early stage of$GA_3$treatment. Secretion of enzyme by $GA_3$ into the surrounding medium was more enhanced in $(1-3,1-4)-{\beta}-glucanases$ than in $(1-3)-{\beta}-glucanase$, The differential response of the enzymes might be related to the physiological role of the enzymes in germination of barley grain.

• Molecules and Cells
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• v.23 no.2
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• pp.207-214
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• 2007

lant ${\beta}$-1, 3-glucanases are involved in plant defense and in development. Very little data are available on the expression of rice glucanases both in developmental tissues and under various stresses. In this study, we cloned and characterized twenty-seven rice ${\beta}$-1, 3-glucanases (OsGlu) from at total of 71 putative glucanases. The OsGlu genes were obtained by PCR from a cDNA library and were classified into seven groups (Group I to VII) according to their DNA or amino acid sequence homology. Analysis of the expression of the twenty-seven OsGlu genes by Northern blotting revealed that they were differentially expressed in different developmental tissues as well as in response to plant hormones, biotic stress, high salt etc. OsGlu11 and 27 in Group IV were clearly expressed only in stem and leaf and were also induced strongly by SA (5 mM), ABA ($200{\mu}M$), and M. grisea. OsGlu1, 10, 11, and 14 were induced earlier and to higher levels in incompatible M. grisea interaction than in compatible one. Taken together, our findings suggest that the twenty-seven rice OsGlu gene products play diverse roles not only in plant defense but also in hormonal responses and in development.

• Journal of Microbiology and Biotechnology
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• v.17 no.8
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• pp.1291-1299
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• 2007

Two ${\beta}$-1,4-glucanases (DI and DIII fractions) were purified to homogeneity from the culture filtrate of a cellulolytic bacteria, Cellulomonas sp. CS 1-1, which was classified as a novel species belonging to Cellulomonas uda based on chemotaxanomic and phylogenetic analyses. The molecular mass was estimated as 50,000 Da and 52,000 Da for DI and DIII, respectively. Moreover, DIII was identified as a glycoprotein with a pI of 3.8, and DI was identified as a non-glycoprotein with a pI of 5.3. When comparing the ratio of the CMC-saccharifying activity and CMC-liquefying activity, DI exhibited a steep slope, characteristic of an endoglucanase, whereas DIII exhibited a low slope, characteristic of an exoglucanase. The substrate specificity of the purified enzymes revealed that DI efficiently hydrolyzed CMC as well as xylan, whereas DIII exhibited a high activity on microcrystalline celluloses, such as Sigmacells. A comparison of the hydrolysis patterns for pNP-glucosides (DP 2-5) using an HPLC analysis demonstrated that the halosidic bond 3 from the nonreducing end was the preferential cleavage site for DI, whereas bond 2, from which the cellobiose unit is split off, was the preferential cleavage site for DIII. The partial N-terminal amino acid sequences for the purified enzymes were $^1Ala-Gly-Ser-Thr-Leu-Gln-Ala-Ala-Ala-Ser-Glu-Ser-Gly-Arg-Tyr^{15}$-for DI and $^1Ala-Asp-Ser-Asp-Phe-Asn-Leu-Tyr-Val-Ala-Glu-Asn-Ala-Met-Lys^{15}$-for DIII. The apparent sequences exhibited high sequence similarities with other bacterial ${\beta}$-1,4-glucanases as well as ${\beta}$-1,4-xylanases.

• Proceedings of the Korean Society of Life Science Conference
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• 2005.04a
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• pp.168-168
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• 2005

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.2
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• pp.121-127
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• 1994

A procedure for the direct detection of (1-3)-$\beta$-glucanase isozymes in electrophoresis gels was developed. The procedure employed the commercial preparation of AZCL-pachyman as a chromogenic substrate for (1-3)-$\beta$-glucanases. The procedure detected the three basic isozymes which have been known to be expressed in germinating barley kernels. A major acidic and a minor isozymes were also detected in germinating kernels. The procedure was proved to be fast, simple and sensitive enough to be used for the analysis of the expression of (1-3)-$\beta$-glucanase isozymes in plant tissues. The detection limit of the procedure for the commercial preparation of Penicillium (1-3)-$\beta$-glucanase was estimated to be as low as 50$\mu$U. The procedure could be used for the investigation of (1-3)-$\beta$-glucanases in laboratories facilitated with ordinary equipments and research personnel.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.11 no.6
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• pp.755-768
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• 1998

Nitrogen and phosphorus are major nutrients in animal feeds which partially remain in the environment as pollution. In addition, nitrogen and phosphorus along with energy are the main nutrients which determine the feed cost. Any decreases in the levels of these three nutrients can contribute to reducing the pollution problem as well as the cost of feed. The nutrient requirements for chickens in the work here reported should allow for the addition of mixed enzymes (phytases, proteases, glucanases, xylanases and others). Such minimal levels of crude protein in the research results which are here reported are 16% for 0-6 weeks of age, 13.5% for 7-12 weeks of age, 11.5% for 13-18 weeks of age for layer type chicks, 13% for layer, 18% for 0-3 weeks of age broiler and 16.5% for 4-7 weeks of age broiler. These research projects have been done without adding enzyme supplements to their experimental diets. The minimal values of phosphorus, shown as available phosphorus, are 0.25% for pullets, 0.09% for layers and 0.25% for broilers with the addition of phytase. The minimum energy requirement (metabolizable energy) for reducing the feed cost could be summarized as 2,750 kcal per kg feed for pullets, 2,800 kcal for layers and 2,700 kcal for broilers.

• Applied Biological Chemistry
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• v.35 no.3
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• pp.165-169
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• 1992

Two types of $endo-{\beta}-1,3-glucanases$ were purified from green malt and their basic characteristics were studied. Molecular weights of glucanase I and glucanase II were estimated, by electrophoresis, to be 35,000 and 28,000, respectively. Purified glucanase I and II showed the highest activity at pH $5.0{\sim}7.0$ and $5.0{\sim}8.0$, respectively. The optimal temperature of purified glucanase I and II was $40^{\circ}C$. Purified glucanase I and glucanase II were stable at $40^{\circ}$ for 60 min and at $50^{\circ}$ for 30 min. All enzymes were inactivited by $AgNO_3$ and $HgCl_2$ while those were not activated by various compounds tried. Km values of glucanase I and II were 1.03 mg/ml, 1.20 mg/ml, respectively.

• Korean Journal Plant Pathology
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• v.12 no.1
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• pp.1-10
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• 1996

Xanthomonas campestris pv. vesicatoria의 감염으로 토마토 잎조직에 $\beta$-1, 3-Glucanases와 chitinases가 합성, 축적되었다. 그러나 접종되지 않은 건전한 잎에서는 위의 두 가지 가수분해 효소는 매우 낮은 수준으로 유지되었고, 이 두 가지 효소는 친화적 상호작용에서보다는 불친화적 상호작용에서 더욱 높은 수준으로 존재하였다. 이것은 $\beta$-1, 3-glucanases와 chitinases가 X. c. pv. vesicatoria의 생육에 대한 방어기작으로서 중요한 역할을 한다는 것을 시사해 주고 있다. Native PAGE 젤 상에서 $\beta$-1, 3-glucanases를 분리한 결과, 병징 발현이나 저항성 발현에 중요한 역할을 하는 것으로 생각되는 산성 isoform Ga 1과 염기성 isoform Gb 1의 isoform bands만 확인되었다. Isoelectric focusing을 이용하였을 때, 적어도 pI 6.4와 pI 8.6을 지닌 두 개의 $\beta$-1, 3-glucanases의 isoform을 확인할 수 있었고, 특히 불친화적 상호작용에서 더욱 뚜렷하게 유도되었다. 이것은 병 진전과정에서 X. c. pv. vesicatoria에 대해 저항성 발현에 관여한다는 것을 나타내고 있다. 산성 chitinase isoform인 Ca 1의 활성은 병원균의 감염이 진전되는 동안 감소하였다. 또한 다섯 개의 염기성 chitinase isoform이 감염된 토마토 잎 조직에서 발견되었는데, 특히 토마토의 방어기작에 관여하여 병원화적 균주 Bv5-4a에 감염된 잎에서만 유도, 축적되었다. Isoelectric focusing(IEF)을 이용한 후 적어도 2개의 산성과 4개의 염기성 chitinase isoform이 감염된 토마토 잎 추출액에서 확인되었다. Native PAGE 젤에서 isoform Cb 1에 해당되는 pI 9.5를 지닌 chitinase isoform은 오직 불친화적 상호작용에서만 확인되었다. 이온이 제거된 Triton X-100을 처리하여 renaturation 시킨 후에 SDS-PAGE 젤 상태에서 23 kDa과 26 kDa을 지닌 2개의 chitinase isoform을 확인하였다.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.10
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• pp.1457-1463
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• 2005

In this research, the possibilities of using canola meal (CM) in place of soybean meal (SBM), and also the effects of multi-enzyme and phytase supplementation on the performance of quails were investigated. For this purpose, soybean meal (44% CP), canola meal (37% CP), phytase (produced from Peniophora luci) and multi-enzyme ($\beta$-glucanases, pectinases, cellulases and hemicellulases) were used. CM was used supplying 0, 25 and 50% of CP from SBM and each of the phytase and multi-enzyme blends were added to the each level. This study was conducted with 675 day old quails (Coturnix coturnix Japonica) in 9 groups with 3 replicates including 25 birds (mixed sex) per replicate. Nine isocalaric and isonitrogenous diets were prepared. The effects of enzymes and CM levels were studied with a 3${\times}$3${\times}$3 factorial arrangement for three CM levels (0, 25 and 50%), three treatments (without enzyme, phytase enzyme and multi-enzyme) and three replicates. While the 25% CM level did not affect the liveweight gain 50% CM level decreased the liveweight gain (p<0.05). Multi-enzyme addition to the 50% CM group increased the liveweight gain compared to the other groups (p<0.05). CM levels and enzyme supplementation had no effect on feed consumption, feed conversion ratio, dressing percentage, viability, tibia ash content, Ca and P contents of tibia ash, viscera weight, gizzard weight and length of growth period. While heart weight and liver weight were not affected by CM levels, but they were affected by enzyme supplementation. CM levels and enzyme supplementation did not affect final liveweight, feed consumption, feed conversion ratio, egg yield, egg weight, shell weight and shell index during laying period. The increase in the CM level lightened the colour of the yolk (p<0.05).