• Journal of Life Science
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• v.19 no.3
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• pp.366-372
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• 2009

In the course of screening of useful enzyme-producing microorganisms from marine sedimentary layers, we isolated 2 amylase producing strains and tested their amylase producing activities. Analyses of 16S rDNA sequences and biochemical methods (BIOLOG) of two isolates showed that they were confirmed to be a gram positive Bacillus sp. and gram negative Pseudoalteromonas sp., respectively. Excellent amylase producing strains were termed Bacillus sp. ST-63 and Pseudoalteromonas sp. ST-140, and further studies were conducted on their amylase producing characteristics. Optimum conditions for cell growth in amylase activity were obtained when the isolate (Bacillus sp. ST-63 and Pseudoalteromonas sp. ST-140) was cultured at $30^{\circ}C$ and pH $7{\sim}8$.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.12 no.1
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• pp.276-280
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• 2011

This study investigated the activation conditions of pancreatic enzymes from porcine pancreas. Duodenum induced the activation of pancreatic protease and lipase in pancreas. When 10% duodenum was added to pancreatic juice and the mixture was incubated at $30^{\circ}C$ for 90 min or at $25^{\circ}C$ for 4 hrs, the activities of pancreatic protese and lipase reached the peak. When the pancreatin was prepared by sequential process of enzymatic activation at $25^{\circ}C$ for 4 hrs, centrifugation, acetone precipitation and freeze-drying, the specific activities of pancreatic protease, lipase and amylase were 136, 116 and 400 U/mg-protein, respectively. The protease, lipase and amylase activities of the prepared pancreatin were 5.4, 58.0 and 16.0 times higher than those of USP standard, respectively.

• Proceedings of the Ginseng society Conference
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• 1984.09a
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• pp.37-43
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• 1984

노화는 모든 다세포 유기물의 특징이다. 노화가 됨에 따라서 효소활성 및 면역반응의 감소와 과산화지질과 지방갈색물질의 축적, 효소와 염색질을 포함하는 단백질 구조의 변화, 호르몬계의 불균형 등이 일어난다. 그렇지만, 노화가 어떻게 일어나는지에 관하여는 현재까지 확실하지 않다. 본 연구진은 노화와 관련된 효소들에 관하여 연구를 하여 왔으며, 노화가 진행되는 동안의 효소의 활성을 유지시켜주거나, 또는 효소의 활성이 감소되는 것을 지연시켜 주는 물질을 찾고자 노력하였다. 그 가운데 하나로서, 고려인삼 추출물을 흰쥐에 기간별로 투여하여 효소활성의 차이, 열에 대한 안정성, 기질에 대한 친화력, 전기 영동 상의 이동성과 면역적인 반응을 대조군과 비교하였다. Glucose-6-phosphate dehydrogenase, 6-phosphog-luconate dehydrogenase, glutathione redutease, glutathion peroxidase와 같은 노화와 관련된 효소들의 활성을 고려인삼 추출물을 1개월간 흰쥐에 ($60{\~}80$g)투여하여 대조군과 비교 조사하였으나, 별 차이가 없었다. 그러나 고려인삼 추출물을 15개월간 투여하였을 때에는 이러한 노화관련 효소들의 활성이 급격히 증가함이 ($70{\~}200\%$) 관찰되었다. 예견된 바와 같이, 효소의 열에 대한 안정성과 기질에 대한 친화력도 증가함이 관찰되었다. 그러나 glucose-6-phosphate dehydrogenase의 경우에서 전기영동상의 차이 및 면역적인 반응은 대조군과 유사하였다. 이상의 결과는 고려인삼 추출물이 노화와 관련된 효소들의 활성이 감소되는 것을 지연시켜줄 수 있으며, 노화를 어느정도 지연시켜 줄 수 있음을 의미한다. 이와 같은 결과를 포함한 실험자료를 국제 인삼심포지움에서 발표할 것이다.$-tocopherol의 항 산화작용을 더욱 효과적으로 촉진 시킬 것으로 생각된다.-L(독성 호르몬-L)의 작용을 억제함으로서 암환자의 체중 감소를 방지하고, 식욕감퇴를 개선할것으로 생각된다.해되었으며, $Rb_{1}$은 장내의 효소와 tetracycline-resistantant bacteria에 의해 Rd와 2 종류의 미확인 물질로 분해되었다.xA_{2}$ synthetase 억제제인 imidazole의 효과와 유사하였다. 4. G-Re는 $1{\times}10^{-5}g/ml$ 이하의 농도에서는 효과가 없으나 $1{\times}10^{-4}g/ml$ 이상의 농도에서 농도의존적으로 유의성 있는 $PGE_{2},\;PGF_{2}{\alpha},\;TXB_{2}$의 생성억제와 함께 6-keto-$PGF_{1}{\alpha}$ 증가를 보였다. 이는 prostacyclin synthetase를 자극하는 serotonin의 효과와 같은 작용으로서 prostacyclin synthetase 억제제인 tranylcypromine에 대하여 길항효과를 보였다. 5. $TxB_{2}$생성억제 작용을 나타내는 ginsenoside들의 효과를 뒷받침하기 위하여 인삼 saponin 성분을 전처치한 patelet rich plasma에서 혈소판 응집시험 결과, ADP로 유도된 혈소판 응집반응에는 모든 인삼 saponin 성분들이 효과가 없었으나 arachidonic acid로 유도된 혈소판 응집반응에는 $G-Rb_{2}$, G-Rc, G-Re의 순으로 농도 의존적인 억제현상을 보였다. 이상의 결과와 같이 인삼 saponin 성분들은 arachidonic acid로부터 cyclooxygenase를

• Proceedings of the KTCVS Conference
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• 1995.10a
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• pp.1-1
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• 1995

• Journal of Life Science
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• v.22 no.6
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• pp.751-759
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• 2012

Microbulbifer sp. was used to acquire the degrading products from Ecklonia cava (DPEC) and the products were investigated to determine the physiological activities. Firstly, 2,2-diphenyl-1-picrylhydrazyl (DPPH) activity and superoxide dismutase (SOD) assay were about 84.1% and 89.6% at 2.5 mg/ml, respectively. In addition, nitrite scavenging ability was shown to be 56.3% at 0.5 mg/ml on pH 1.2. ${\alpha}$-Glucosidase inhibitory activity was increased in a dose-dependent manner and was about 58.7% at 2.5 mg/ml. To determine the influence of DPEC on alcohol metabolism, the generating activity of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) were measured. Facilitating rates of ADH and ALDH activities by DPEC were 123.3% and 215.2% at 2.5 mg/ml, respectively. For analyses of anti-wrinkling and whitening effects, its elastase and tyrosinase inhibitory activities were measured and were about 73.1% and 42.2% at 2.5 mg/ml, respectively. These results indicated that DPEC has valuable biological attributes owing to its antioxidant, nitrite scavenging, and alcohol metabolizing activities and ${\alpha}$-glucosidase, elastase, and tyrosinase inhibitory activities.

• Journal of the Korean Society of Food Science and Nutrition
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• v.37 no.1
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• pp.42-47
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• 2008

Prevention of postprandial hyperglycemia is important, as it is implicated in the development of macro- and microvascular complications associated with diabetes. An inhibitor of ${\alpha}$-amylase which acts in the first step of carbohydrate digestion, is expected to be a suppressor of postprandial hyperglycemia. This study investigated the porcine pancreatic ${\alpha}$-amylase inhibitory activity of the extracts from buckwheat (Fagopyrum esculentum) flower, leaf, stem and grain. Flower, leaf, stem and grain of buckwheat were extracted by water and ethanol (40%, 70%, 100%), respectively. Flower and leaf extracts were more effective ${\alpha}$-amylase inhibitors than stem and grain extracts in all tested solutions. Ethanol extracts were more effective than water extracts or powders on the ${\alpha}$-amylase inhibitory activities. At concentrations of $0.5%{\sim}10%$ (w/w, starch basis), the flower extracts of 40%, 70% and 100% ethanol lowered the enzyme activity by about 90% and the results were similar to the values of acarbose. At the same concentrations, the leaf extracts of 100% ethanol lowered the enzyme activity by about 90%. These results suggest that buckwheat flower and leaf ethanol extracts may delay carbohydrate digestion and lower postprandial hyperglycemia.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.803-806
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• 1993

The properties of proteolytic enzymes from the fruit of Broussonetia Kazinoki Siebold were investigated. The protease activity of the enzymes from the fruit of Broussonetia Kazinoki Siebold was 1.6 unit. The optimum temperature and pH of the enzymes were $60^{\circ}C$ and 7.0, respectively. The enzymes were stable at pH values from 6 to 8 for 1 hr. at $37^{\circ}C$ of incubation and also retained all activity after incubation for 1 hr. at $60^{\circ}C$. The enzyme preparations showed strong activities toward hemoglobin and collagen.

• Korean Journal of Microbiology
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• v.27 no.3
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• pp.237-244
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• 1989

A soluble intracellular protease from cells of Pseudomonas carboxydovorans, a carboxydobacterium, grown on nutrient broth was purified 68-fold in five steps to better than 95% homogeneity with a yield of 2.4% using azocasein as a substrate. The enzyme activity was not detected from cells grown on pyruvate, succinate, acetate, or CO as a sole source of carbon and energy. The molecular weight of the native enzyme was determined to be 53,000. Sodium dodecyl sulfate-gel electrophoresis revealed the purified enzyme a monomer. The enzyme was found to be a serine-type protease. The enzyme activity was inhibited completely by several divalent cations such as $Cd^{2+}, Cu^{2+}, Hg^{2+}$, and $Fe^{2+}$. The enzyme was also inhibited by EGTA, but was stimulated by iodoacetamide. The optimal pH and temperature for the enzyme reaction were found to be 8.0 and $50^{\circ}C$, respectively. The enzyme was inactive on CO dehydrogenase.

• Korean Journal of Food Science and Technology
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• v.47 no.6
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• pp.698-703
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• 2015

The elderly or patients with masticatory disturbance and deglutition dysfunctions, may have difficulty in chewing or biting foods with a hard texture. Thus, softening of the texture of foods using hemicellulase immobilized by the nanoencapsulation technique was examined in this study. Burdock was cut into cylindrical-shaped samples, which were immersed in distilled water and non-coated or coated enzymes for 48 h at $4^{\circ}C$. The hardness of the treated samples decreased compared to the control. Microstructural observations revealed that the cells in the non-coated burdock were destroyed after 24 h. From the point of view of enzyme activity, the initial activity of the non-coated enzymes was higher than that of the coated enzymes. However, the enzyme activity was not significantly affected by the immersion time. Therefore, it appears that the encapsulation technique for enzymes may be useful for softening the texture of foods.

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.1
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• pp.41-46
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• 2004

A correlation between fibrinolytic activity and microflora in Korean traditional soybean fermented food was investigated. The fibrinolytic activities of traditional soybean pastes and commercially processed samples were 2.42$\pm$1.01 unit/g and 1.58$\pm$0.98 unit/g, respectively. The cell density of Bacillus in traditional soybean pastes was about 10$^{7}$ CFU/g and its commercially processed one was 10$^{6}$ CFU/g. Acid producing bacteria, fungi and yeast group were higher in commercially processed one. The correlations of fibrinolytic activity and microflora in traditional and commercial Doenjang were positively correlated in Bacillus ($R^2$≒ 0.69), negatively correlated in fungal group ($R^2$≒0.40), and there were no significant correlations in acid forming bacteria and yeast group ($R^2$<0.16). Fibrinolytic activities in Meju and Koji were 6.54$\pm$1.97 unit/g and 1.46$\pm$0.43 unit/g respectively, and were positively correlated with Bacillus. Yeast and acid forming bacteria were grown by 5∼6 decimal induction during fermentation period of Doenjang, but Bacillus, fungal cells and fibrinolytic activity were nearly stable. Results indicate that fibrinolytic activity of Doenjang depends on enzyme induction in Meju or Koji processing by Bacillus, Doenjang fermentation process.