• 한국염색가공학회지
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• 제24권1호
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• pp.18-26
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• 2012

In this work, colorants extraction process from gromwell was studied for making powder form of colorants by solving the high viscosity problem of gromwell extracts. In order to do that, sugar extracted together with colorants must be pre-extracted. For sugar decomposition, gromwell roots were pretreated with various enzyme solutions. The total sugar content of pre-extract with enzyme solution was measured. Accordingly, the effects of enzyme type and pretreatment condition on sugar decomposition were investigated to find appropriate enzyme(amylase, hemicellulase, pectinase) and enzyme activity (100~1000unit), pre-extracted time(3~24hr). Color characteristics and dye uptake of dyed fabrics were evaluated. Gromwell colorants were assessed for their potential antimicrobial activities, which possibly expand their end use as functional pigments. The efficiency of removing sugar was increased in the order of hemicellulase, pectinase, amylase, $H_2O$. Gromwell colorants powder yield was in the range of 4.4% to 9.8% depending on pretreatment enzyme. Gromwell colorants produced RP color on the silk and wool fabrics with good dye uptake. Antimicrobial activity of gromwell colorants will greatly increase its potentiality for applying as functional natural colorants in the future.

• 한국응용과학기술학회지
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• 제15권3호
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• pp.21-26
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• 1998

Polyvinyl alcohol[PVA] is useful for the production of water-soluble packaging, paper, textile sizes. PVA and Chitosan are known as biodegradable polymers. PVA/chitosan blend films were prepared by solution blends method in the weight ratio of chitosan for the purpose of useful biodegradable films. Thermal and mechanical properties of PVA/chitosan blend films such as DSC, impact strength, tensile strength and morphology by SEM were determined. As a result, The ratio of 10.0wt% PVA/chitosan blend films were similar to PVA. Blend films were completely degraded pH 4.0 better than 7.0, 10.0 in the buffer solution. Also, Blend films were rapidly degraded enzyme(${\beta}-glucosidase$) solution better than pH solution by Enzymolysis.

• 한국식품과학회지
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• 제22권4호
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• pp.426-433
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• 1990

Bacillus subtilis HP-4의 ${\beta}-galactosidase$를 추출, 정제하여 효소의 고정화조건 및 고정화 효소의 특성을 조사하였다. B. subtilis를 배양하여 얻은 조효소액을 acetone분획 DEAE-cellulose에 의한 ion exchange chromatography, Sephadex G-100에 의한 gel filtration과정을 통하여 정제하였던 바 약 68% 정제되었으며, 이때의 회수율은 19.9%이었다. 본 효소의 최적 고정화조건은 2%(w/v)의 sodium alginate농도, 15%(v/v)의 효소농도, 그리고 2%,(w/v)의 $CaCl_2$ 농도에서 2시간 교반하였을 때 이었다. 고정화 효소의 최적온도와 pH값은 각각 $55^{\circ}C$와 6.5이었다. 고정화 효소의 활성은 Hg이온과 Cu이온에 의하여 저해되었으며, EDTA, 2-mercaptoethanol, KCN 등의 금속이온 그리고 보호제에 의한 영향은 없었다. 고정화 효소의 ONPG와 유당에 대한 $K_m$값과 $V_{max}$값은 각각 $1.82{\times}10^{-2}M$과 $2.94{\times}10^{-2}M$ 그리고 $3.57{\times}10^{-8}mole/min$과 $1.68{\times}10^{-7}mole/min$이었다. 고정화 효소를 $4^{\circ}C$에서 40일간 저장 후 잔존활성과 5회 재사용 후 잔존활성을 조사한 결과는 각각 95%와 81%이었으며, 탈지유(4.8% 유당)와 5% 유당용액에서 $50^{\circ}C$, 9시간 반응시켰을 때 유당분해율은 각각 51%와 43%이었다.

• Korean Journal of Acupuncture
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• 제18권1호
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• pp.11-20
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• 2001

댑싸리하고초 약침액을 이용하여 phase II detoxification 효소인 quinone reductase (QR 및 GST) 유도, GSH 생성량, phase I 효소 cytochrome P4501A1 활성억제, 발암물질 B[a]P-DNA adduct 형성의 저해효과 등을 측정하였다. QR 생성 유도를 Hepa1c1c7로 실험한 결과, 댑싸리하고초 약침액및 열수추출액 모두에서 유도 되었으며, 농도가 높아질수록 유도율이 더 높게 나타났으며, GSH와 GST의 유도율도 약침액에서 나타났다. 댑싸리하고초 약침액 $5{\times}$에서 45.2%의 cytochrome P4501A1 효소활성 저해효과를 측정할 수 있었다. 또한 B[a]P-DNA binding 저해효과를 실험한 결과, 약침액 $3{\times}$ 농도에서 45.0%의 저해효과가 있었다. 이상의 결과에 의하면 댑싸리하고초 약침액은 암억제 물질로서의 기능을 충분히 발휘할 것으로 사료된다.

• 한국미생물·생명공학회지
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• 제9권4호
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• pp.213-218
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• 1981

순수분리정제된 $\beta$-galactosidase의 분자량은 Sephadex G-200 gel filtration법에서 130,000이며 SDS-polyacrylamide gel electrophoresis에서 130,000외에 70,000이 확인되어 이 효소는 70,000인 2개의 subunit로 구성되어 있다고 판단되었다. 효소의 안정pH는 4.5~7.0이며 효소활성의 최적 pH는 4.7 최적온도는 5$0^{\circ}C$였다. 효소활성 및 안정제로 1가, 2가 금속ion을 필요로 하지않았으며 C $u^{++}$ 1mM에서 59%, galactose 100mM에서 48% 저해되었다. 5% lactose용액, 시유 및 10% skim milk 용액에 이 정제된 $\beta$-galactosidase 10units/$m\ell$를 사용하여 5$0^{\circ}C$에서 4시간 동안 반응시켰을 때 lactose가 각각 69.5%. 88.7% 및 72.6%가 glucose와galactose로 전환된 결과를 얻었다.

• 한국균학회지
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• 제14권3호
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• pp.189-194
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• 1986

한국산 표고균(菌)의 생리적 조사의 일원으로서 이 균주(菌株)가 목재에서 생장시 필요로하는 목재분해 효소들의 특징 및 생성경향을 조사하였다. 각 효소들의 유도를 위한 배지로서는 각각 단일의 특정탄소원을 첨가한 배지를 사용하였고 이때 추출한 조효소를 효소용액으로 사용하였으며 이들 효소에 대한 최적온도 및 최적 pH등의 조건을 조사하였다. 또한 이 균주가 목재구성성분을 분해하는 기작을 간접적으로 추정하기 위하여 복합배지 및 통방배지 내에서의 각 효소생성 양상을 측정하였다. 이 균주가 목재성분을 분해할 때에는 cellulose와 hemicellulose의 하나인 xylan을 초기에 분해하여 이용하고, 조금지나서 pectin 질을 분해함을 알수있었다. 또한 이들기질들은 서로 상호작용에 의해 분해가 좀더 원활하게 이루어지게 하는데 효과가 있었다.

• 동의생리병리학회지
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• 제18권3호
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• pp.874-879
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• 2004

Alakaline phosphatase (ALP)- or horseradish peroxidase (HRP)-antibody conjugate was used frequently on the immunological detection methods such as enzyme-linked immunosobent assay (ELISA), immunobolt, immunohistochemistry. The classical enzyme-antibody coupling method by one-step (direction) injection of glutaraldehyde bring into being disadvantage such as low sensitivity of antigen detection because of homopolymers. This study was modified with the dialysis glutaraldehyde method to provide simple coupling through E-amino residues present in most protein. The dialysis glutaraldehyde coupling effects were better than the classical one-step glutaraldehyde injection in antigen detection of ELISA and immunobolt. Optimal dose of the dialysis glutaraldehyde solution was 0.10-0.25 %. This results suggest that the dialysis glutaraldehyde coupling method can readily applied to antigen detection of in vitro and in vivo.

• 한국식품영양학회지
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• 제9권3호
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• pp.253-258
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• 1996

Stabilities of sweets potato f-amylase on various reagents were studied. The enzyme was stabilized by bovine serum albumin, Triton X-100 and 2-mercaptoethanol of 0.04%. Among them, bovine serum albumin was the most effective. And enzyme stability was increased by using the deairated solution. The enzyme activity was remained 0% in the absence of glycerol, 25% in the presence of 20% glycerol and 50% in the presence of 40% glycerol at 37$^{\circ}C$, for 15 hours in pH 11. SDS inhibited the enzyme, and 2-mercaptoethanol and dithiothreitol stabilized it.

• 한국수산과학회지
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• 제28권6호
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• pp.728-735
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• 1995

The peptidyl prolyl cis-trans isomerase(PPlase, EC 5.2.2.8) from Bacillus stearothermophilus SIC1 was extracted from the cells treated with by lysozyme. PPlase was purified from the cell extracts by heat treatment, ammonium sulfate precipitation, ion exchange chromatography and finally gel filtration (FPLC). The purity of purified the enzyme after Superose 12 column chromatography was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE). The molecular weight of the purified PPlase was estimated as 18,000 by SDS-PAGE. The 39 amino acid residues from the N-terminus were determined by the protein sequencer. The enzyme showed the optimum pH at 8.0 and was stable at the range of pH 7.0 to 8.0. The enzyme was considerably stable after heat treatment at $60^{\circ}C$ for 30 minutes, and the enzyme was quite stable up to $65^{\circ}C$. The presence of the PPlase in the refolding solution accelerated the isomerization rate of the assay peptide.

• 한국연초학회지
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• 제7권1호
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• pp.75-84
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• 1985

A strain of Trichoderm sp. J-30 which strongly products cellulase to reduce the content of cellulose in the stem of leaf tobacco was isolated from leaf tobaco. The Trichoderma sp. J-30 was identified as Trochoderma voride. The cellulase from this strain was purified with the physico-chemical methods and treated in the culled stem of leaf tobacco. The results obtained were summarized as follows. 1. Optimal pH of the enzyme was at pH 5.0. 2. The enzyme shooed a higher activity at $40^{\circ}C$ and its thermal stability began to decrease at $60^{\circ}C$. 3. The enzyme activity was promoted by the metal ions such as $Ca^{2+}, Mg^{2+}, Pb^{2+}and\;Zn^{2+}.$ 4. When the culled stem of leaf tobacco was applied with the 3% of the enzyme solution at $40^{\circ}C$ for 3 days. 15 to 17% of cellulose contents decreased, 12 to 13% of total sugar increased and the filling power was increased by 10-13% in the sample.