• 한국식품과학회지
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• 제48권3호
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• pp.201-207
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• 2016

메밀껍질은 메밀 알곡보다 유효성분이 많음에도 불구하고 식품학적 가치가 떨어져 대부분 폐기되고 있다. 따라서 이를 기능성 식품소재로 활용하기 위해 효소분해하여 기능성 올리고당을 생산하고 이들의 특성을 분석하였다. 올리고당 생산을 위한 최적 가수분해조건은 셀룰로스 분획의 경우 pH 5.0, $40^{\circ}C$, 기질농도 4%로 결정되었으며, 헤미셀룰로스 분획은 pH 5.0, $40^{\circ}C$, 30 unit으로 결정되었다. 최적 분해조건을 이용하여 72시간 효소분해 후 얻은 올리고당의 생산량을 측정한 결과, 셀룰로스와 헤미셀룰로스 분획으로부터 얻은 올리고당의 수율은 각각 132.37 g/kg 및 393.04 g/kg이었다. 또한 각 분획의 올리고당 함량을 측정한 결과, 포도당, 자일로스, xylobiose, xylotriose, cellobiose 및 cellotriose가 검출되었다. 올리고당(OSC, OSH)의 산화방지 활성을 측정한 결과, OSC는 분해시간이 증가할수록 산화방지 활성은 감소한 반면 OSH는 증가하였다. 또한 메밀껍질로부터 생산된 올리고당 첨가 시, 모든 비피더스 균주의 생육이 control에 비해 증가하여 프리 바이오틱 효과가 있음을 알 수 있었다. 이상의 연구결과, 효소분해에 의해 메밀껍질로부터 올리고당을 생산할 수 있었으며, 산화방지와 프리바이오틱 효과가 있음을 확인하였다. 따라서 목적에 따라 효소의 처리시간 및 방법을 다양화한다면 기능성식품으로의 활용이 더 높아질 것으로 예상된다.

• Fisheries and Aquatic Sciences
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• 제7권2호
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• pp.51-57
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• 2004

Total phosphorus contents in rice bran and soybean meal were determined to be 5.81 and $2.77\%$, respectively, and $97.2\%$ of phosphorus in rice bran and $66.4\%$ in soybean meal were presented as phytate phosphorus. Optimum pH condition for hydrolysis of phytate in rice bran and soybean was determined to be in the pH range of 3.7 and 5.3. The highest activity of phytase for hydrolysis of phytate in both samples was determined to be at $55^{\circ}C$ for rice bran and $55-60^{\circ}C$ for soybean. Hydrolysis of phytate in soybean meal at pH 5.0 increased with the co-reaction or consecutive reaction with protease; however, in rice bran hydrolysis decreased with co-reaction with protease. Phytate degradation of soybean meal in the presence of pepsin at pH 2.5 showed higher than that of rice bran. Phytate degradation of rice bran in the presence of trypsin or pancreatin at pH 7.0 increased the activity around 2-times compared with the activity in the absence of trypsin or pancreatin. The results of this study suggest that hydrolysis of phytate in rice bran or soybean meal with phytase and protease may provide an alternative process for the preparation of aquacultural feed with a low level of organic phosphorus.

• 대한약침학회지
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• 제17권1호
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• pp.44-50
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• 2014

Objectives: This study was undertaken to isolate a fibrinolytic enzyme from the snake venom of Gloydius blomhoffii siniticus and to investigate its enzymatic characteristics and hemorrhagic activity as a potential pharmacopuncture agent. Methods: The fibrinolytic enzyme was isolated by using chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and fibrin plate assay. The characteristics of the enzyme were investigated using fibrin plate assay, protein hydrolysis analysis, and hemorrhage assay. Its amino acid composition was determined. Results: The fibrinolytic enzyme with the molecular weight of 32kDa (FE-32kDa) from Gloydius blomhoffii siniticus showed a fibrin hydrolysis zone at the concentration of 0.2 mg/mL in the fibrin plate assay. The fibrin hydrolysis activity of the enzyme was inhibited completely by ethylenediaminetetraacetic acid (EDTA), ethyleneglycoltetraacetic acid (EGTA), and 1, 10-phenanthroline, thiothreitol and cysteine, and partially by phenylmethanesulfonylfluoride (PMSF). Metal ions such as $Fe^{2+}$ and $Hg^{2+}$ inhibited the fibrin hydrolysis completely, but $Zn^{2+}$ enhanced it. FE-32kDa hydrolyzed ${\alpha}$-chain but did not hydrolyze ${\beta}$-chain and ${\gamma}$-chain of fibrinogen. High-molecular-weight polypeptides of gelatin were hydrolyzed partially into low-molecular-weight polypeptides, but the extent of hydrolysis was limited. FE-32kDa induced hemorrhage beneath back skin of mice at the dose of $2{\mu}g$. Conclusions: FE-32kDa is a ${\alpha}$-fibrin(ogen)olytic metalloprotease that requires $Zn^{2+}$ for fibrinolytic activity and causes hemorrhage, suggesting that the enzyme is not appropriate for use as a clinical pharmacopuncture.

• Preventive Nutrition and Food Science
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• 제14권4호
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• pp.323-328
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• 2009

Cryotin F could be used for hydrolyzing shrimp byproducts into bioactive ingredients, which could be used as value-added products. The objective of this study was to investigate the optimum condition for antioxidative activities of the enzymatic hydrolysate produced with Cryotin F using response surface methodology with central composite rotatable design. Shrimp byproducts (shells and heads) were hydrolyzed with Cryotin F. The experimental ranges of the independent variables for 20 experimental runs were 28.2-61.8${^{\circ}C}$ reaction temperature, pH 6-10 and 0.5-5.5% enzyme concentration. The degree of hydrolysis for the reaction products was measured. Their antioxidative activities were measured using 1,1-diphenyl-2-picryl-hydrazyl (DPPH) scavenging activity and Fe-chelating activity. The experimental method with central composite rotatable design was well designed to investigate the optimum condition for biofunctional ingredients with antioxidative activities using Cryotin F because of their high R2 values of 0.97 and 0.95 for DPPH-scavenging activity and Fe-chelating activity, respectively. Change in enzyme concentration did not significantly affect their antioxidative activities (p<0.05). Both DPPH scavenging activity and chelating activity against Fe for the enzyme hydrolysates were more affected by the pH of enzyme hydrolysis than by their action temperature. DPPH-scavenging activity was higher at acidic pH than alkali pH, while chelating activity against Few was inversely affected. Hydrolysate of shrimp byproducts showed high antioxidative activities depending on the treatment condition, so the optimum treatment of enzymatic hydrolysate with Cryotin F and other proteases can be applied to shrimp byproducts (shells) and other protein sources for biofunctional ingredients.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVI)
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• pp.360-363
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• 2005

This study was a method that used a hydrolysis for increasing the efficacy of alcohol decrease from Hovenia dulcis extract. The best pH was 2.0 to obtain a maximum activity at fixed reaction temperature and time. At pH 2.0, reaction temperature $80^{\circ}C$ and reaction time 4 hr gave the highest activity which was 124.2% of control. This is very simple and efficient method to increase the efficacy of alcohol decrease from Hovenia dulcis extract. The mechanism that increases the efficiency of alcohol decrease be examined through hydrolysis.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2005년도 생물공학의 동향(XVII)
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• pp.530-534
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• 2005

This work was a method that used an acid hydrolysis for increasing the efficacy of decreasing alcohol concentration from Hovenia dulcis extract. The best pH was 2.0 to obtain a maximum alcohol dehydrogenase activity at fixed reaction temperature and time. At pH 2.0, reaction temperature $80^{\circ}C$ and reaction time 4hr gave the highest activity which was 124% of control. The bioactive compound, (+)-dihydromyricetin, content increased to 30% after acid hydrolysis. This is very simple and efficient method to increase the efficacy of decreasing alcohol concentration from Hovenia dulcis extract. The mechanism that increase the efficiency of alcohol decrease be examined through hydrolysis.

• 한국식품영양학회지
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• 제9권2호
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• pp.167-175
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• 1996

This studies were conducted to select optimal enzyme that produced hydrolysate from soybean, and to evaluated functionality of hydrolysate. Soybean powder was suspended with water and hydrolyzed by seven commercial proteases. Hydrolysate produced with protease from Bacillus subtilis showed the highest inhibition effect on the activity of angiotension converting enzyme(ACE), and the condition of enzymatic hydrolysis was 5cA substrate concentration, 0. l% enzyme concentration, 4 hour hydrolysis time. Under above optimum condition, soybean was hydrolyzed with protease from Bacillus subtilis yielding a DH (degree of hydrolysis) of about 49%. Hyrophobicity of hydrolysate was not correlated with the inhibition effect on ACE activity. The functionality of hydrolysate was significantly influenced by pH. Solubility of hydrolysate at alkali solution was greater than that at acidic solution.

• KSBB Journal
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• 제6권2호
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• pp.157-166
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• 1991

The structural properties of cellulose are significantly changed with the progress of hydrolysis reaction. The effects of changes on such properties of cellulosic substrate as crystallinity, amicessibility of enzyme to the active site of cellulose surface, and particle size on the kinetics of enzymatic hydrolysis have been studied. Among those physical studies, the apparent surface active site of cellulose particle was found to have the most significant effect on the hydrolysis kinetics. Based on the experimental results, the adsorption affinity of enzyme and hydrolysis rate were mainly influenced by the surface roughness of cellulose particle. The extent of accesssible active site may be expressed as the change of particle diameter. The Langmuir isotherm was proposed in terms of enzyme activity to explain the actual action of enzyme protein.

• KSBB Journal
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• 제14권4호
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• pp.511-516
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• 1999

유지의 가수분해시, 반응온도, 금속이온, pH, 교반속도, 물-유지의 무게비 및 효소량 등의 환경 및 조성인자가 효소 Lipase-OF의 역가 및 가수분해특성에 미치는 영향을 규명하였다. 융점이 낮은 유지의 경우 Lipase-OF의 활성이 가장 높은 온도는 37$^{\circ}C$ 근방이었으나 융점이 4$0^{\circ}C$ 이상의 온도 범위에서는 유지의 종류에 관계없이 온도가 상승하면 Lipase-OF의 활성이 급격히 감소하여 $65^{\circ}C$ 이상에서는 효소의 활성이 정지되었다. 교반속도를 150, 250, 350, 450, 550 및 650 rmp으로 변화시켜가면서 유지의 가수분해실험을 수행하여 350 rpm 이하에서는 교반속도가 상승하면 가수분해율도 상승하였으나 교반속도 350 rpm 이상에서는 교반속도 상승에 대한 가수분해율의 변화를 찾아볼 수 없었다. 유지와 물의 무게비를 9 : 1에서 1 : 9까지 변화시켜가면서 가수분해실험을 수행하여 일정한 가수분해 시간에서 가수분해율이 가장 높은 무게비가 1 : 1 근방의 값임을 규명하였다. 금속 이온 중 $Ca^{2+}와\;Mg^{2+}$ 이온이 가수분해율 상승에 기여하였다. 금속이온이 없는 경우에 비하여 $Ca^{2+}$또는 $Mg^{2+}$ 이온 농도가 100 ppm 근방의 값일 때 2 내지 3%의 가수분해율 증가효과를 나타내었다. Lipase-OF에 대한 최적 pH는 7근방이었다. pH가 산성쪽으로 감소하면 가수분해율도 감소하였으며 알칼리쪽으로 증가하여도 가수분해율이 감소하였다. 기질의 0.00075 wt% 와 0.1 wt% 범위내에서 Lipase-OF량이 가수분해율에 미치는 영향을 규명하였다. 효소량 0.013 wt% 이하에서는 효소량이 증가하면 가수분해율도 증가하였으나 0.013 wt% 이상에서는 효소량이 증가하여도 가수분해율은 증가하지 않았다. Lipase-OF의 가수분해율에 미치는 환경 및 조성인자의 영향에 대한 실험을 통하여 최적온도는 37$^{\circ}C$, 최적 pH는 7, $Ca^{2+}\;또는\;Mg^{2+}$의 최적농도는 100 ppm, 최적교반속도는 350 rpm, 유지와 물의 최적무게비는 1 : 1 및 최적 효소량은 유지의 0.013 wt%임을 규명하였다.

• Bulletin of the Korean Chemical Society
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• 제34권9호
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• pp.2741-2746
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• 2013

The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.