• Journal of Animal Science and Technology
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• 제49권1호
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• pp.129-136
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• 2007

본 실험은 한우 육단백질의 가수분해물로부터 항고혈압 활성을 측정하기 위하여 실시한 것으로서 한우 등심과 우둔으로부터 추출한 myosin B를 pepsin으로 가수분해하여 가수분해물들의 전기영동 결과, 가열처리와 가수분해 시간의 증가에 따라 단백질의 소실이 증가하였다. 항 고혈압 활성을 측정한 결과 10 ug/ml의 희석된 가수분해물의 ACE 억제효과는 1시간 이상 가수분해 시키면 약 40%의 억제율을 가졌다. 가수분해물 원액으로 ACE 억제효과를 살펴본 결과에서는 등심이 우둔보다 높았으며 (p<0.05), 비가열 가수분해물이 가열한 가수분해물 보다 억제율이 높게 나타났다 (p<0.05). 또한, 가수분해 시간별 처리구에서는 1시간 이상 가수분해 시키면 약 70% 이상의 억제율을 갖는 것으로 나타나 한우의 myosin B를 1시간 이상 가수분해하면 ACE 억제율이 증진되는 것으로 사료된다.

• 미생물학회지
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• 제31권1호
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• pp.93-98
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• 1993

수계생태계에서 유기물질의 순환을 이해하기 위하여 팔당호에서 종속영양 활성도와 세균세포의 효소활성의 계절절 변화를 연구하였다. 팔당호 I 의 glucose 전환시간은 수층, 퇴적토에서 2-1,300 시간, 17-170 시간, protein hydrolysate 는 5-900 시간, 15-240 시간, acetic acid 는 4-350 시간, 15-230 시간으로 계절적인 변화를 나타냈다. Glucose, protein hydrolysate, acetate 각각의 호흡율은 수층에서 23-32%, 38-41%, 22-28%로 나타났고 퇴적토에서는 34%, 61% and 41% 로 나타났다. 이 결과로 3가지 유기물질 종류 모두가 수층보다 퇴적토에서는 높은 율로 호흡됨을 알 수 있었다. 한편 세균의 $\alpha$-glucosidase, $\beta$-glucosidase, N-acetyl-$\beta$-D-glucosaminidase, aminopeptidase 활성력을 살펴본 결과 수층에서는 효소 각각에 대해 32-44%, 31-32%, 18-34% 61-67% 의 범위를 나타내었고 퇴적토에서는 34%, 40%, 23% 65%로 나타났다.

• 한국수산과학회지
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• 제34권6호
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• pp.577-583
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• 2001

황복의 소화효소의 변화과정을 부화직후부터 부화 후 65일까지 측정 하였다. 발육단계에 따른 소화효소의 발현과 활성의 변화에서 $\alpha-amylase$ 비활성은 전장 10mm에서 0.0493U/mg의 최소값을 나타낸 후, 전장 19mm를 전후하여 0.1480 U/mg의 최대값을 나타냈다. Trypsin과 pepsin 비활성은 전장 16mm에서 각각 0.0264U/mg, 0.0258U/mg 와 전장 24mm에서 0.0178U/mg, 0.0201 U/mg의 값을 가지는 두 번의 peak를 보였고, 이 시기에 황복 자치어의 성장률도 증가하는 경향을 보였다. 또한, trypsin과 pepsin의 비활성을 비교하여 보면, 자어기인 전장 $4\~5mm$와 치어 II기인 전장 $19\~24mm$에서는 pepsin이 높았고, 치어 I 기인 전장 $11\~16mm$와 유어기인 전장27 mm 이후에서는 trypsin이 높았다.

• 한국과학교육학회지
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• 제29권8호
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• pp.923-933
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• 2009

본 연구에서는 고등학교 과학 교과서에 제시된 'pH가 효소의 활성에 미치는 영향'에 대한 실험의 문제점을 분석하였다. 본 실험은 16종의 교과서 중 5개의 교과서에 소개되어 있으며, 실험 조건을 분석하였다. 교과서 분석 결과 산성 조건은 pH 3 이하이고, 염기성 조건은 pH 11이상이었다. 우선 교과서에 제시된 실험조건을 토대로 pH 조건을 다양하게 하여 실험을 실시하였다. 교과서에 제시된 것처럼 완충 용액을 사용하지 않고 pH 조건을 맞춰주었을 때, 침의 완충 작용으로 pH 범위로 pH가 맞춰지는 현상이 발견되었다. 그래서 본 연구에서는 pH 2에서 13인 완충 용액을 이용하여 효소 활성에 대한 실험을 수행하였다. pH 2에서 4사이에서 시료는 파란색을 나타내었고 pH 5부터 pH 8 에서는 색이 없어졌다. 이는 효소활성으로 인해서 녹말이 소화된 것을 나타낸다. pH가 9에서는 옅은 파란색이 나타났는데 이는 효소활성이 감소한 것을 나타낸다. 그러나 pH가 10이상으로 더 증가했을 때 효소의 비활성으로 인해 파란색이 더 짙어질 것이라는 기대와 달리, pH 10일 때 파란색이 더 옅어졌고, pH 11이상에서는 색이 없어졌다. 이는 이렇게 강한 염기성 조건에서 효소가 활성화된다고 학생들이 잘못해석하도록 영향을 미칠 수 있는 사안이다. 분석 결과 ${I_3}^-$, ${I_5}^-$는 녹말-요오드 화합물에서 녹말 나선 안에 존재하는 폴리요오드화 이온의 기초가 되며 이들이 색을 띄게 되는데, 이들이 $OH^-$와 반응하여 $I^-$, HOI, ${IO_3}^-$로 분해되기 때문으로 해석되었다.

• Journal of Life Science
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• 제9권1호
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• pp.26-34
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• 1999

A thermostable pullulanase has been isolated and purified from Thermus caldophilus GK-24 to a homogeneity by gel-filtration and ion-exchange chromatography. The specific activity of the purified enzyme was 431-fold increase from the crude culture broth with a recovery of 11.4%. The purified enzyme showed $M_{r}$ of 65 kDa on denaturated and natural conditions. The pI of the enzyme was 6.1 and Schiff staining was negative, suggesting that the enzyme is not a glycoprotein. The enzyme was most active at pH 5.5. The activity was maximal at $75^{\cire}C$ and stable up to $95^{\cire}C$ for 30 min at pH 5.5. The enzyme was stable to incubation from pH 3.5 to pH 8.0 at $4^{\cire}C$ for 24hr. The presence of pullulan protected the enzyme from heat inactivation, the extent depending upon the substrate concentration. The activity of the enzyme was simulated by $Mn^{2+}$ ion, }$Ni^{2+}$, $Ca^{2+}$, $Co^{2+}$ ions. The enzyme hydrolyzed the ${\alpha}$-1,6-linkages of amylopectin, glycogens, ${\alpha}$, ${\beta}$-limited dextrin, and pullulan. The enzyme caused the complete hydrolysis of pullulan to maltotriose and the activity was inhibited by $\alpha$, $\beta$, or $\gamma$-cyclodextrins. The $NH_{2}$-terminal amino acid sequence [(Ala-Pro-Gln-(Asp of Tyr)-Asn-Leu-Leu-Xaa-ILe-Gly-Ala(Ser)] was compared with known sequences of various sources and that was compared with known sequences of various sources and that was different from those of bacterial and plant enzymes, suggesting that the enzymes are structurally different.

• Applied Microscopy
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• 제17권2호
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• pp.55-71
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• 1987

To investigate the effects of lead on the electron transport system and ultrastructure of mouse kidney mitochondria, various lead acetate concentrations were treated in vitro and respiration rate, enzyme activities were measured. Ultrastructural changes at state IV respiration were also observed. To compare with in vivo experiments, mouse were injected intraperitoneally of 100 mg lead acetate per kg body weight and state IV respiration rate and enzyme activities were measured. Ultrastructure of renal proximal tubular cells were also observed. In in vitro treatement, decreased state IV respiration, decreased enzyme activities, ruptured membranes and inhibition of condensed to orthodox transformation were observed. In in vivo treatment, decreased state IV respiration and decreased enzyme activities were observed after 24 hrs of i.p. injection. Cytochrome c oxidase activity showed twice the inhibition compared to NADH-CoQ reductase activity at 24 hrs. Continuous decreased state IV respiration was observed after 48 and 72 hrs of injection, however, the enzyme activities were increased to control level. Lead-protein complex which probably inhibits the toxic effects of lead appeared. To conclude, dominant effect of lead on the electron transport system appeared at cytochrome c oxidase activity, and the increased enzyme activities may be a result of appearance of lead-protein complex.

• Nutritional Sciences
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• 제7권1호
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• pp.35-40
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• 2004

This study was performed to evaluate the effect of iron supplementation on iron-deficiency-related indices, oxidative stress and antioxidative enzyme activity in female marathoners. Fourteen teenage female marathoners participated in the study. Subjects were divided into two groups: mild anemic and control, depending on their hemoglobin (Hb) level. The mild anemic group had significantly lower RBC count and hematocrit (Hct) and Hb levels compared to the control group. The mild anemic group (〈12.5g Hb/dI, n=7) was given iron supplements (60mg Fe/day) for four weeks during the summer training period. RBC count, Hct and Hb levels showed an increasing tendency through iron supplementation, and significant differences in these variables between the anemic and control groups disappeared in the post-period. There was no difference in plasma malondialdehyde (MDA) between the anemic and control groups. However, catalase (CAT) and glutathione peroxidase (GPx) activity were significantly higher in the anemic group. The significant difference in enzyme activity between the groups disappeared in the post-period. In addition, superoxide dismutase activity significantly decreased after iron supplementation. In conclusion, antioxidative enzyme activity was up-regulated in an anemic condition and mild iron supplementation decreased the antioxidant enzyme activity of female marathoners while improving their anemic condition.

• Preventive Nutrition and Food Science
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• 제2권1호
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• pp.55-60
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• 1997

A lysosomal and matrix degrading enzyme $\beta$-glucuronidase activity was measured in BALS/c mice fed high and low Ca in combination with the i.p. adminstration of calcium-regulating hormones including parathyoid hormone(PTH), calcitonin(CT) and cholecalciferol(Vit D). After feeding experimental diets for five weeks, mice were sacrificed by cervical dislocation and the enzyme was fluometrically measured at 440nm. $\beta$-Glucuronidase activity was inhibited by high calcium in the diet. in addition, vitamin D also inhibited the enzyme activity in the serum regardless of the level of dietary calcium. In contrast, PTH has shown to stimulate the enzyme at all the levels of dietary calcium. Calcitonin, and inhibitor of PTH action for bone resorption, revealed to curb PTH effect in this enzyme, whereas CT stimulated the action of vitamin D in the serum. The above results led us to conclude that osteoclastic bone resorption and senile osteoporosis may be reduced by adequate dietary calcium and vitamin D.

• 한국축산식품학회지
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• 제18권2호
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• pp.97-106
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• 1998

Antioxidant enzymes such as catalase (CAT), glutathione peroxidase (GSH-Px) and superoxide dismutase (SOD) are known to inhibit oxidative reactions by incativating compounds responsible for the formation of ree radicals. SOD transforms superoxide radical into hydrogen peroxide which is precursor to active free radicals. CAT reduces hydrogen peroxide to water. GSH-Px reduces hydroperoxides to corresponding alcohols. Antioxidant enzyme activities of muscle are different by animal species age, stress and exercise, muscle type and part, conditions of post mortem, storage and processing which are related to oxidative deterioration I muscle foods as well as oxidative defence in living systems. Antioxidant enzyme systems are enhanced rather than weakened in aging skeletal muscle. Red muscle contains higher antioxidant enzyme activity than white muscle. The antioxidant enzyme activities of poultry are higher in leg than in breast, and those of beef are higher in redder and more unstable muscles. It is clear that the effectiveness of the antioxidant enzyme in muscle foods seems to be influenced by meat processing operations. Both GSH-Px and CAT are inactivated by heat processing NaCl also influence the efficiency of the antioxident enzymes since its presence diminishes their catalyitc activity.

• Food Science and Biotechnology
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• 제17권4호
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• pp.873-877
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• 2008

Native soy protein isolate (SPI) was hydrolyzed with 4 different proteolytic enzymes, including bromelain, papain, Neutrase, and Flavourzyme. SPI hydrolysates with the degree of hydrolysis (DH) in range of 6 to 15% were prepared by each enzyme. The angiotensin 1 converting enzyme (ACE) inhibitory and the antioxidant activities of the SPI hydrolysates, such as superoxide dismutase-like activity and inhibition of the linoleic acid autoxidation, were evaluated. Overall, as the DH increased, all evaluated bioactivities of the SPI hydrolysates significantly increased. The significantly highest ACE inhibitory and antioxidant activities were found in hydrolysates made with papain and bromelain, respectively. SPI hydrolysates by Flavourzyme showed the significantly lowest activity in all tested bioactivities. The results suggested that ACE inhibitory and antioxidant activities of SPI hydrolysates were determined by the DH and by the enzyme used.