• 제목/요약/키워드: soybean peroxidase

검색결과 57건 처리시간 0.017초

Soybean peroxidase의 추출공정 및 안정성 특성 (Extraction Process and Stability Characteristics of Soybean Peroxidase)

  • 서경림;이은규
    • KSBB Journal
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    • 제13권5호
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    • pp.599-605
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    • 1998
  • Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

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콩나물 Peroxidase를 이용한 포도당의 효소적 분석 (Enzymatic Determination of Glucose Using Soybean Sprouts Peroxidase.)

  • 이민경
    • 생명과학회지
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    • 제8권4호
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    • pp.416-420
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    • 1998
  • 콩나물 줄기로부터 추출, 정제한 peroxidase는 glucose oxidase와 함께 guaiacol을 기질로 사용하여 포도당의 분석에 사용되었다. peroxidase는 DEAE-Sephacel ion exchange column chromatography를 통해 얻은 분획이 조효소액에 비해 specific activity가 10.8배 증가되었고 수율은 11.3%였다. 정제된 peroxidase와 glucose oxidase를 이용한 포도당 분석의 최적 pH는 5.5였고 최적온도는 $40^{\circ}C$로 나타났으며 포도당 양의 증가에 따라 효소활성은 증가되었으며 반응시간과의 관계에서도 직선을 보여 주었다. 그리고 L-cysteine과 dithiothreitol과 같은 환원제는 포도당 분석에 이용되는 glucose oxidase와 콩나물 peroxidase의 활성을 저해하는 것으로 나타났다.

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대두종자의 자반병 감염과 Peroxidase 활성도변화 (The Change of Peroxidase Activity in Soybean Seed Followed by Infection with Cercospora kikuchii)

  • 박원목;고영희;유영준;이장용
    • 한국응용곤충학회지
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    • 제21권1호
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    • pp.23-26
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    • 1982
  • Cercospora kikuchii에 의해서 발병된 대두종자의 부패균에 대한 획득저항성기작을 구명코자 본 연구를 실시하였다. 1. 대두의 건전종자, 자연열개종자, 인위적 상처종자 및 자반병 감염종자재의 전단백질 함량에는 차이가 없었으나 peroxidase활성도는 감염종자에서 월등히 높았다. 2. 대두의 건전종자와 자반병 감염종자의 종피 및 자엽내의 단백질함량에는 큰 차이가 없었으며 peroxidase활성도는 자엽에서는 차이 가 없었으나 종피에서 건전한 종피보다 자반병에 감염된 종자가 2.5배 정도 높은 활성도를 보였다. 3. Polyphenol oxidase는 대두의 건전종자의 자반병 감염종자 모두 활성도가 너무 낮아 측정할 수 없었다. 4. 전기영동에 의한 peroxidase isozyme pattern은 건전종자와 감염종자간에 차이가 없었다. 5. 자반병에 대한 저항성기작은 자반병균에 의하여 대주종피 자체내에서 생화학적 방어기작이 더욱 활성화 하였으며 peroxidase활성도의 증가는 병원균에 대한 반응으로 사료된다.

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Acifluorfen 의 경엽처리(莖葉處理)가 대두(大豆) 및 바랭이의 엽조직(葉組織)에서 Peroxidase 활성(活性)에 미치는 영향 (Effects of the Foliar Applied Acifluorfen on the Peroxidase Activity in Leaf Tissue of Soybean (Glycine max Merr.) and Crabgrass (Digitaria adscendens (L.) Scopol.))

  • 김태완;강병화
    • 한국환경농학회지
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    • 제7권1호
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    • pp.52-57
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    • 1988
  • acifluorfen이 대두(大豆)와 바랭이의 경엽(莖葉)에서 peroxidase의 활성(活性)에 어떻게 영향(影響)을 미치는가를 구명(究明)하여 얻어진 결과(結果)를 요약(要約)하면 다음과 같다. 1. Peroxidase 활성(活性)은 처리농도(處理濃度)가 높을수록 높았으며 처리시기(處理時期)가 늦을수록 낮았다. 2. 1.5부엽기(復葉期)에 처리(處理)했을 때는 신생엽(新生葉)인 2부엽(復葉)의 활성(活性)이 높았으나, 2.5부엽기(復葉期)에 처리(處理)했을 경우는 신생엽(新生葉)인 3부엽(復葉)의 활성(活性)이 오히려 낮았다. 3. 1.5부엽 (復葉) 처리(處理)의 신생엽(新生葉)인 2부엽(復葉)에서의 peroxidase 활성(活性)이 2.5부엽(復葉)의 처리(處理)의 2부엽(復葉)보다 높았다. 4. 모든 처리엽(處理葉)이 necrosis와 leaf burning현상이 나타났지만, 처리(處理) 14日(일) 후(後)에는 거의 정상으로 회부(回復)되었다. 5. 바랭이는 처리(處理) $1{\sim}2$일후(日後) peroxidase 활성(活性)이 현저히 증가하였고, 5 일후(日後)는 급격히 감소하였다. 이는 바랭이가 acifluorfen 처리후(處理後) $3{\sim}7$ 일내(日內)에 모두 고사(枯死)하였기 때문이었다.

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콩나물 Peroxidase의 효소적 특성 (Enzymatic Characterization of Peroxidase from Soybean Sprouts)

  • 박인식;이민경
    • 한국식품영양과학회지
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    • 제27권6호
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    • pp.1143-1147
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    • 1998
  • Enzymatic characterization of peroxidase(E.C. 1.11.1.7) from soybean sprouts was investigated. The optimum pH of the purified peroxidase was 7.0 and relatively stable at pH 6.0~7.0. And the optimum temperature was 50oC. The enzyme was most active with guaiacol as a substrate, followed by (+)catechin, pyrogallol and p phenylenediamine. The Km values for guaiacol and H2O2 were 4.2mM and 2.5mM, respectively. L Ascorbic acid and 2 mercaptoethanol greatly inhibited the enzyme activity, while Cu2+, Co2+ and Ni2+ activated the enzyme.

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콩나물 Peroxidase의 열안정성과 재활성화 (Thermostability and Reactivation of Peroxidase from Soybean Sprouts)

  • 박인식;이민경;길지은
    • 한국식품영양과학회지
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    • 제28권1호
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    • pp.81-86
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    • 1999
  • The factors affecting thermostability and reactivation of peroxidase from soybean sprouts(Glycine max L.) were investigated. The enzyme was the most stable at pH 7.0 and below 60oC. Thermostability of the enzyme was reduced by addition of sodium chloride and saccharides. The partially inactivated enzyme by heat treatment at 75oC for 10 min was reactivated up to 211.5% at the optimal reactivation condition. The optimal pH and temperature for reactivation of the enzyme were pH 9.0 and 40oC, respectively. The reactivation was completely inhibited by addition of sulfhydryl reagent such as L cysteine.

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Sequential Induction of Ethylene, Lipoxygenase, and Ascorbate Peroxidase in Senescing Soybean Callus

  • Ha, Mi-Young;Kim, Do-Kyun;Kim, Soon-Young;Kang, Bin-G.;Oh, Seung-Eun
    • BMB Reports
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    • 제29권6호
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    • pp.564-568
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    • 1996
  • Bursts of ethylene production occurred in twice at an early exponential (EEP) and prestationary (PSP) phases, respectively, during growth of callus tissue isolated from the root of soybean seedlings. The second burst of ethylene production at PSP was smaller in magnitude than the earlier one at EEP, but was followed by increases in both guaiacol peroxidase (GuPOX) and ascorbate peroxidase (AsPOX). The increase in AsPOX activity was also preceded by an increase in lipoxygenase (LOX) activity. Treatment of the tissue with the ethylene antagonist 2,5-norbonadiene (NBD) resulted in substantial reduction in LOX and AsPOX activities during this period. GuPOX activity was reduced only slightly, if any, by NBD. Role of ethylene in the sequential induction of LOX and AsPOX in senescing callus tissue is discussed.

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쥐의 대두 단백질 섭취가 국소 뇌허혈/재관류 후 뇌경색 크기와 항산화효소 활성도에 미치는 영향 (Effect of Dietary Soybean Protein on Cerebral Infarction Size and Antioxidant Enzyme Activities in Rat Focal Brain Ischemia Model)

  • 이희주
    • Journal of Korean Biological Nursing Science
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    • 제10권1호
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    • pp.1-10
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    • 2008
  • Purpose: The purpose of this study was to investigate the cerebral infarction size, antioxidant enzyme activities and lipid peroxidation changes after 6 weeks of dietary soybean protein intake in a rat focal brain ischemia model. Method: Weaning Sprague-Dawley rats were fed with either modified AIN-93G diet containing casein 20% (control), 20% soybean protein isolate-based diet (S20), or 40% of soybean protein isolate-based diet (S40) for 6 weeks. The animals were subject to right middle cerebral artery occlusion for 2 hr. After 24 hr of recirculation, the rats were sacrificed. Antioxidant enzymes activities of superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) and thiobarbituric acid reactive substance (TBARS) level in the right brain were also measured. Result: There were no significant differences in the right cortical infarction volume, TBARS level, SOD and CAT activities among the three groups whereas the GPx activities of the S20 group were significantly higher than those of the control group (p=.02). Conclusion: Our results suggest that 20% of soybean protein may have a modulating effect on GPx and possibly have some protective effect against oxidative stress although it may enough to decrease cerebral infarction volume in rat focal brain ischemia model.

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Heterologous Expression of Phanerochaete chrysoporium Glyoxal Oxidase and its Application for the Coupled Reaction with Manganese Peroxidase to Decolorize Malachite Green

  • Son, Yu-Lim;Kim, Hyoun-Young;Thiyagarajan, Saravanakumar;Xu, Jing Jing;Park, Seung-Moon
    • Mycobiology
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    • 제40권4호
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    • pp.258-262
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    • 2012
  • cDNA of the glx1 gene encoding glyoxal oxidase (GLX) from Phanerochaete chrysosporium was isolated and expressed in Pichia pastoris. The recombinant GLX (rGLX) produces $H_2O_2$ over 7.0 nmol/min/mL using methyl glyoxal as a substrate. Use of rGLX as a generator of $H_2O_2$ improved the coupled reaction with recombinant manganese peroxidase resulting in decolorization of malachite green up to $150{\mu}M$ within 90 min.

풋콩의 품질향상을 위한 마이크로파에 의한 블랜칭 (Effect of Microwave Blanching on the Improvement of the Qualities of Immatured Soybean)

  • 최용희;정호덕;유종근
    • 한국식품영양과학회지
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    • 제28권6호
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    • pp.1298-1303
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    • 1999
  • For the purpose of improving the qualities of immatured soybean(Seoklyang), the effects of table height (0, 5, 10, 15mm) and time(60, 66, 72, 78 sec) for microwave blanching on physicochemical properties were investigated. Enzyme inactivities lipoxygenase and peroxidase for all there conditions were more de creased than for control and water blanching. Enzyme activity of each conditions was expressed as percentage on the enzyme activity of control. Lipoxygeanse activity and peroxidase activity of immatured soybeans were about 20% and 10% levels, respectively. Also the color showed the higher L(lightness), b(yellowness), chroma(brightness) values, but the lower a(redness) and hue angle. Vitamin C content was worse than for control, but was better than for water blanching. Hardness with a few exceptions showed the higher value for control.

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