• 한국작물학회지
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• 제40권2호
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• pp.250-254
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• 1995

분리한 보리호분층을 이용하여 $(1-3)-{\beta}-glu-canase$와 $(1-3,1-4)-{\beta}-glucanase$의${\;}GA_3$에 대한 반응특성을 조사하였다 $GA_3$ 처리에 의해 호분충과 배양액 내의 단백질 함량, $(1-3)-{\beta}-glucanase{\;}$및${\;}(1-3,1-4)-{\beta}-glucanase$ 활성 등이 모두 증가하였다. 그러나 $GA_3$ 처리에 의한 효소활성 및 효소분비 증가 정도는 효소에 따라 큰 차이를 보였다. $(1-3,1-4)-{\beta}-glucanase$가${\;}(1-3)-{\beta}-glucanase$보다 효소활성 증가 정도와 분비증가 정도 모두 컸다. 이와 같은 결과는 발아초기 $(1-3,1-4)-{\beta}-glucanase$의 중요한 생리작용과 관계가 있을 것으로 생각되었다.

• Molecules and Cells
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• 제23권2호
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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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• 제17권8호
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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.

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2005년도 국제학술심포지움 The 44th Annual Meeting of Korean Society for Life Science
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• pp.168-168
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• 2005

• 한국작물학회지
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• 제39권2호
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• pp.121-127
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• 1994

(1-3)-$\beta$-glucanase 동위효소의 발현 양상을 등 전점 전기영동 젤에서 직접 검출 확인할 수 있는 방법을 개발하였다. 개발된 방법은 시판되고 있는 (1-3)-$\beta$-glucanase활성 측정용 염료착색 기질을 이용하였다. 본 방법은 신속, 간편하며 보리 종자에서 발현되는 것으로 알려져 있는 모든 (1-3)-$\beta$glucanase 동위효소를 검출할 수 있을 정도로 민감하고 특이적이었다. 시판되고 있는 Penicillium(1-3)-$\beta$-glucanase에 대한 활성 검출 한계단위는 50 $\mu$U 정도로 추정되었다. 따라서, 본 방법은 특별한 시설이나 연구 인력을 확보하고 있지 않는 연구실에서 식물체의 (1-3)-$\beta$-glucanase발현에 대한 단백질 수준에서의 연구를 수행하는데 유용하게 이용될 수 있을 것으로 생각된다.

• 생명과학회지
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• 제13권3호
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• pp.355-358
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• 2003

식물 병원성 진균인 Rhizoctonia solani에 대한 길항능이 있는 Trichoderma 계열의 미생물 균주를 선별하였다. R. solani의 성장을 저해하는 능력이 우수한 균주를 선별하기 위하여 일차적으로 PDA 평판에서 inhibition zone을 측정하였고, 병원성 진균의 세포벽을 용해시킬 수 있는 세포외 효소인 glucanase 및 chitinase 활성을 분석하였다. 4∼5 mm 이상의 inhibition zone을 보여주었고, glucanase 및 chitinase 활성이 우수한 Trichoderma sp. UK-3와 T. viride 균주들을 선별할 수 있었다.

• Asian-Australasian Journal of Animal Sciences
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• 제11권6호
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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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• 제35권3호
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• pp.165-169
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• 1992

녹맥아로부터 $endo-{\beta}-1,3-glucanase$를 추출하여 각종 수지로써 정제하여 glucanase I과 glucanase II의 존재를 확인하였고, 정제한 두 효소의 특성에 대하여 실험한 결과, 두 정제 효소의 분자량은 각각 35,000과 28,000으로 추정되었으며 최적 pH는 5.5이었고 pH 안정 범위는 각각 달랐다. 두 정제효소의 최적 온도는 glucanase I, II 다 같이 $40^{\circ}C$이었으며 glucanase I에 비해 glucanase II가 열에 다소 안정하였다. 그리고 $AgNO_3$와 $HgCl_2$와 같은 화합물은 효소활성을 저해하였다. Laminarin을 기질로 하여 측정한 Km값은 glucanase I, II 각각 1.03 mg/ml, 1.20 mg/ml이었다.

• 한국식물병리학회지
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• 제12권1호
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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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• 제18권10호
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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).