• Applied Biological Chemistry
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• 제29권3호
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• pp.266-272
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• 1986

맥주맥(麥灌麥) 장려품종의 원맥(原麥)과 맥아(麥芽)에서 수용성(水溶性) ${\beta}-glucan$함량(含量)은 각각(各各) $1.4{\sim}4.0%$와 $0.3{\sim}0.6%$범위(範圍)였다. 원맥(原麥)의 ${\beta}-glucan$함량(含豊)은 품종(品種), 재배지역(載培地域) 및 질소질비료(窒素質肥料) 수준(水準)의 영향(影響)을 많이 받는 것으로 나타났다. 원맥(原麥)의 ${\beta}-glucan$함량(含量)은 점도(粘度)와 고도(高度)의 정(正)의 관(關)을 보였으며 , 단백질함량(蛋白質含量)과 total gum함량(會量)에 대(對)하여는 각각(各各) 부(負)의 상관(相關)을 나타내었다. 맥아(麥芽)의 ${\beta}-glucanase$활성(活性)은 점도감소(粘度減少)의 상대시간(相對時間)으로 표시(標示)할 때 $11.0{\sim}20.0$초(秒)였으며, 품종(品種), 재배지역(栽培地域) 및 질소비료(室素肥料) 수준(水準)의 영향(影響)을 많이 받았으며, 제맥아중(製麥芽中) ${\beta}-glucanase$활성(活性)은 제6일(第6日)째 이후(以後)부터 최고수준(最高水準)을 유지하였다. 맥아(麥芽) ${\beta}-glucanase$활성(活性)은 맥아(麥芽)의 잔존(殘存) ${\beta}-glucan$함량(含量)과 부상관(負相關)을 추출수량(抽出收量)과는 정상관(正相關)을 보였다. 맥아(麥芽)의 단백질함량(蛋白質含豊)은 추출수량(抽出收量)과 부상관(負相關)을, 효소력가(酵素力價)와 정상관(正相關)을 보였다.

• 환경위생공학
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• 제10권2호
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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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• 제26권5호
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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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• 제19권8호
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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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• 제5권1호
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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.

• 농업과학연구
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• 제39권3호
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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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• 제19권4호
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• pp.288-290
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• 2004

효모의 종류에 따라 세포벽의 composition이 다른 것으로 알려져 있으나 이에 대한 체계적인 연구는 아직 이루어지지 않고 있다. 본 연구에서는 한국 유전자은행 (KCTC)과 한국미생물 보존센터 (KCCM)에서 구입한 15종류의 효모를 $Glucanex^{(R)}$ 200G로 처리한 후 생균수를 측정하여 상대적인 저항성을 비교하였다. 그 결과 Trigonopsis variabilis나 Sporidiobolus pararoseus는 $\beta$-glucanase에 대한 저항성이 높았으며 Pichia stiptis나 Filibasidium cpasuligenum은 $\beta$-glucanase에 대한 저항성이 낮았다. $\beta$-glucan의 함량이 높은 세포는 높은 농도의 $\beta$-glucanase 농도에서도 저항성을 가지므로 이를 바탕으로 여러 효모의 세포벽의 상대적인 $\beta$-glucan 함량을 추정할 수 있다.

• 미생물학회지
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• 제44권1호
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• pp.69-73
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• 2008

대두가 발효된 청국장에는 미생물, 다양한 효소와 생리활성물질이 존재한다. 청국장의 탄수화물을 분해하는 cellulase에 대한 연구는 많지 않다. Oligosaccharide는다양한 생리활성을 지니고 있다. Congo red test 및 활성염색을 통해, 효소액이 cellulase를 포함하는 것을 확인했다. 청국장 발효 균주 Bacillus licheniformis B1이 분비하는 cellulase활성의 최적 pH와 온도는 각각 10과 $40^{\circ}C$이었다. TLC분석을 통해 효소액은 carboxymethyl cellulose (CMC)를 분해하여 2탄당 이상을 생성함을 확인하였다. 본 균주를 이용해서 제조한 보리 청국장에서는 효소의 활성이 증가되었다. 본 균주의 cellulase 유전자를 클로닝하여 분석한 결과, 본 효소는 ${\beta}$-1,4-glucanase였으며, 전체 coding 영역 $10{\sim}460$번째 아미노산 영역 중, 32군데서 polymorphism을 보였다.

• Journal of Microbiology and Biotechnology
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• 제20권3호
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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.

• 한국유기농업학회지
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• 제9권2호
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• pp.55-67
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• 2001

본 논문의 목적을 위한 외인성 효소 즉 Phytase, $\beta$-glucanase, pentosanase는 전 세계적으로 양돈사료에 첨가제로서 광범위하게 사용하고 있다. 이러한 효소의 화학적 효과는 이해가 잘 되고 있다. 하지만 돼지에서 이러한 효소들의 효과에 대해서는 아직까지 논란의 여지가 있다. Phytase는 곡류내 존재하는 피틴태 인의 이용성을 증가시킬 수 있어 배설되는 분 중 인의 오염도를 낮출 수 있고 사료내 사용하는 무기태 인의 양을 감소시킬 수 있다. 또한, 보리와 귀리에 존재하는 $\beta$-glucanase와 호밀과 밀에 존재하는 용해성 Pentosans과 같은 효소들은 양돈사료에서 찾을 수 있는 항영양소 인자들을 분해하는 효과가 있다. 그래서 비전분과당류들의 소화율을 증가시키는 결과를 초래한다. 앞으로 이 분야의 연구는 현재 효소들의 효율적인 사용, 효과적인 다른 생산품의 개발 그리고 열 안정성 효소들의 개발들을 포함하고 있다.