• Title/Summary/Keyword: 산화효소

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Antioxidant Activities of Cedrela sinensis Hydrolysates Prepared Using Various Enzymes (효소 종류에 따른 참죽 추출물의 산화방지 효과)

  • Oh, Min Hui;Jang, Hye Lim;Lim, Ye Jin;Yoon, Kyung Young
    • Korean Journal of Food Science and Technology
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    • v.47 no.4
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    • pp.413-418
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    • 2015
  • This study was conducted to analyze the functional component contents and antioxidant activities of Cedrela sinensis extracts hydrolyzed using four different enzymes. The yield of Viscozyme extract was the highest among the samples, and all enzymatic extracts, except for the commercial glucoamylase (AMG) extract, had significantly higher total polyphenol and flavonoids contents compared to the non-enzymatic extract (p<0.05). Viscozyme extract showed the highest 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity and $Fe^{2+}$ chelating ability among the samples. All enzymatic extracts showed high>90% 3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical scavenging activity, and there was no significant difference between the enzymatic and non-enzymatic extracts. The reducing power of the extracts using Shearzyme or Viscozyme was significantly higher than that of the other samples (p<0.05). Therefore, the results indicated that all enzymatic extracts (especially Viscozyme extract), except for the AMG extract, showed high antioxidant activity compared to the non-enzymatic extract. These result suggested that the enzymatic extracts of C. sinensis can be used in functional foods.

DISTRIBUTION OF NITRIC OXIDE SYNTHASE ISOFORMS IN PERIORAL EXOCRINE GLANDS IN RATS (흰쥐 구강주위 외분비선에서 산화질소 합성동위효소의 분포)

  • Jeong, Jong-Cheol;Kim, Sun-Hun;Ryu, Sun-Youl
    • Journal of the Korean Association of Oral and Maxillofacial Surgeons
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    • v.26 no.3
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    • pp.284-292
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    • 2000
  • 내인성 산화질소는 산화질소 합성효소에 의하여 합성되며 여러 분비선에서 다양한 기능을 하리라 추측되고 있다. 구강주위 외분비선은 형태적으로 유사하나 분비물의 성분과 분비량은 서로 달라 이들 조직에서 산화질소 동위효소의 분포와 기능을 추론함은 흥미 있는 일이다. 또한 구강주위 외분비선과 분비선의 지배신경의 산화질소동위효소의 분포에 관한 보고는 희박하다. 본 연구는 흰쥐구강 주위 외분비조직, 즉 3대 타액선, 혀의 소타액선, 누선 그리고 구강점막의 피지선과 지배신경 및 신경절에서 eNOS와 nNOS의 분포를 면역조직화학 방법에 의하여 관찰하여 다음의 결과를 얻었다. nNOS는 악하선신경절, 대타액선의 분비도관 주위의 신경절후신경섬유, 혀의 소타액선 주위의 신경절후섬유, 누선에서 강한 양성반응을 보였다. nNOS는 대타액선과 근상피세포에서 중등도의 양성반응을 보였고 이중 이하선에서 반응이 가장 약하였으며, 피지선의 분비관에서 약한 반응을 보였다. 그러나 상교감신경절과 삼차신경절, 소타액선의 분비관 및 대,소 타액선의 선포에서는 반응이 매우 미약하거나 관찰되지 않았다. eNOS는 혈관의 내피세포와 대타액선의 분비관, 누선의 분비관 및 선포에서 강한 양성 반응을 보였고, 근상피세포에서 중등도의 반응을, 피지선에서 약한 반응을 보였다. 모든 신경절과 신경섬유에서 eNOS의 반응은 음성이었고 타액선의 일부 선포에서는 미약한 면역반응을 보였다. 이상의 결과 eNOS에 의해 합성된 NO는 악안면영역의 외분비선에서 혈류량의 조절과 분비도관의 기능 조절에 관여하고, nNOS에 의한 NO는 외분비선의 자율신경계에서 신경전달물질로의 기능과 분비도관에서의 분비기능 조절에 관여함을 시사하였다.

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Effects of Fermented Mulberry Leaves (Morus alba L.) on Oxidative Modification of Antioxidnat Enzymes (항산화 효소의 산화적 변형에 뽕잎 발효물이 미치는 영향)

  • Kang, Jung Hoon
    • Journal of the Korean Applied Science and Technology
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    • v.36 no.3
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    • pp.985-994
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    • 2019
  • Muberry (Morus alba L.) leaves fermented with Hericium erinaceum mycelium (MA-HE) were assessed for the protection against oxidative modification of antioxidant enzymes, Cu,Zn-superoxide dismutase(SOD) and ceruloplasmin(CP). MA-HE were shown to significantly inhibited oxidative modifications and inactivations of Cu,Zn-SOD and CP induced by peroxyl radical. Antioxidant activity of MA-HE evaluated using peroxyl radical scavenging assays. MA-HE showed 44.03% of peroxyl radical scavenging activity at $100{\mu}g/mL$. Thus, MA-HE protect the antioxidant enzymes from oxidative damage by the scavenging peroxyl radicals. The results suggested that MA-HE was effectively removed reactive oxygen species in cells, thereby protecting cytotoxicity caused by oxidative stress.

Electrochemical Properties of Polypyrrole-Glucose Oxidase Enzyme Electrode: 1. An Influence of Glucose Oxidase on Redox Behavior of Enzyme Electrode (Polypyrrole-Glucose Oxidase 효소전극의 전기화학적 특서: 1. 효소전극의 산화환원에 대한 Glucose Oxidase의 영향)

  • 김현철;구할본;사공건
    • Journal of the Korean Institute of Electrical and Electronic Material Engineers
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    • v.13 no.6
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    • pp.520-525
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    • 2000
  • Glucose oxidase was immobilized in polypyrrole by electrosynthesis. The enzyme had an influence on the redox properties of a complex enzyme electrode. In the cyclic voltammograms of the enazyme electrode new peaks were appeared at the potential around 0.7V vs. Ag/AgCl in additional to the typical peaks for polypyrrole. The more immobilized the stronger the peaks became. During the cycling the pH of electrolyte solution was decreased to about 4.4 The reason for that is to be the proton released from the carboxyl in the glucose oxidase in order to keep on a charge neutrality of the oxidized enzyme. This fact suggests that the new peaks in the voltammograms are caused by the redox of glucose oxidase. In the AC impedance spectrum analysis of the electrode the diffusion of electrolyte anion was limited because of chained structure of the enzyme. The faradic impedance was large since the glucose oxidase is an insulator. Therefore when glucose oxidase is entrapped the enzyme should be limited in amount. Because the growth of the polypyrrole is accompanied both charge transfer and mass transport. For the traditional electrosynthesis that means amount of enzyme present in the electrode is limited to as much as film growable.

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The effect of L-Ascorbic Acid on the Oxidative Reaction of Lysine in Collagen. (Collagen 분자 중의 lysine 산화반응에 미치는 비타민 C의 영향)

  • 김미향
    • Journal of Life Science
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    • v.14 no.3
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    • pp.478-483
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    • 2004
  • In a model reaction using lysyl oxidase purified partilally from bovine aorta, effect of L-ascorbic acid AsA on the oxidative reaction of lysine in collagen was investigated. Addition of Ash to the reaction mixture under aerobic conditions resulted in the decrease of enzymatic activity. In order to examine the specificity of AsA in the oxidative reaction of lysine, other reductants including A derivatives instead of AsA were added to the reaction mixture. Thiol such as glutathione had no effect on the activities of lysyl oxidase. on the other hand, it was observed that erythorbic acid, which was a stereoisomer of AsA, had the same inhibitory effect on this oxidative reaction as AsA. Moreover, by the addition of 3,4-dihydroxybenzoate, which was structural analog of AsA, the activities decreased in a similar manner to that of AsA. These results indicate that the regulatory effect of AsA on lysyl oxidase is attributed to characteristics of the structure. From the determination of Ash remained in the reaction mixture, it is shown that AsA concentration remarkably decreased by lysyl oxidase of the reaction mixture. It is hypothesized that endiol groups reduces the enzyme-bound $Cu^{+2}$ required for further progress of the reaction, and suggests that AsA regulates specifically the reduction of $Cu^{+2}$ required to oxidize lysyl oxidase. This findings support that AsA has an important regulatory role on the oxidative reaction of lysine and on changes of collagen cross-links with aging.

Characteristics of Glucose Oxidase Reaction of Onion Juice (양파 착즙액과 포도당 산화효소의 반응 특성)

  • Choi, Bong-Young;Lee, Eun-Mi;Kim, Young-Ran;Kim, Hyun-Jong;Chung, Bong-Woo
    • Korean Journal of Food Science and Technology
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    • v.35 no.3
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    • pp.417-422
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    • 2003
  • The onions are considered to be a favorable functional source of beverage because they contain much sugar and various nutrients, and they are juicy vegetable. Recently, consumers have a new trend to take functional foods with health benefits. To meet this need, this study was the basic research to establish a manufacturing process of functional onion beverage by glucose oxidase. Glucose oxidase catalyzes reaction of glucose oxidation and makes generation of gluconic acid. Kinetics of the reaction was also investigated, and maximum glucose consumption rate $(V_{max})$ of $26.1{\times}10^{-2}\;g/L{\cdot}min$ and $K_m$ of 5.84 g/L were obtained. Optimum conditions were obtained when the glucose oxidase catalyzed reaction was carried out at temperature of $25^{\circ}C$, agitation rate of 450 rpm and aeration rate of 4 vvm in a 2.5 L jar fermentor. Finally, the enzyme reactor was 10-times scaled up and a similar glucose oxidation performance was achieved in the scaled-up reactor.

Performance Enhancement of Biofuel Cell by Surface Modification of Glucose Oxidase using Ferrocene Carboxylic acid (페로신카르복시산을 이용한 글루코스 산화효소의 표면개질에 의한 바이오 연료전지 성능향상)

  • JI, JUNGYEON;CHRISTWARDANA, MARCELINUS;CHUNG, YONGJIN;KWON, YONGCHAI
    • Journal of Hydrogen and New Energy
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    • v.27 no.5
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    • pp.526-532
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    • 2016
  • In this study, we synthesized a mediator immobilized biocatalyst([FCA/GOx]/PEI/CNT) by surface modification using ferrocene carboxylic acid(FCA), and evaluated its performance as anode catalyst for biofuel cell. Through the application of FCA on glucose oxidase (GOx), the free amine groups on the lysine residue of GOx surface reacted with carboxylic acid of FCA and make amide bond between GOx and FCA. As the result of that, the electron transfer of catalyst was increased up to 1.91 times($0.468mA{\cdot}cm^{-2}$) than the catalyst without surface modification (GOx/PEI/CNT), and high maxium power density of $1.79mA{\cdot}cm^{-2}$ was gained.

Antioxidant Activity of Soy-sprout Extracts Prepared by Enzyme and Ultra High Pressure (효소 처리와 초고압 처리에 의한 콩나물 추출물의 항산화 활성)

  • Sung, Hea Mi;Kim, Sook Jeong;Kim, Kyoung Mi;Yun, Su Kyoung;Jung, Hyun Jung;Kim, Tae Yong;Wee, Ji Hyang
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.43 no.8
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    • pp.1228-1235
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    • 2014
  • We investigated the antioxidant activities and effects of soy-sprout extracts (SE) against $H_2O_2$-induced oxidative stress in HepG2 cells. The major free amino acids were asparagine, valine, pheylalanine, histidine, isoleucine, and leucine in SE. Both soy-spout extract by enzyme (SEE) and soy-spout extract by ultra high pressure (SEP) showed higher contents compared with soy-sprout water extract (SEW). The total polyphenol and isoflavone contents were highest in SEE. SEE had the highest DPPH and ABTS radical scavenging activities as well. To determine the effects of SE on $H_2O_2$-induced oxidative damage, cell viability was measured using XTT assay. Pre-treatment with SEE and SEP significantly increased cell viability compared with $H_2O_2$-treated control cells by 29% and 32%, respectively. These results indicate that SEE and SEP possess antioxidant activity.

A Study on the Mechanism of Calcium Binding Inhibition of Cardiac Sarcoplasmic Reticulum by Oxygen Free Radicals (산소대사물에 의한 심장근 Sarcoplasmic reticulum의 칼슘운반 억제 기전에 관한연구)

  • Kim, Hae-Won;Chung, Myung-Hee;Kim, Myung-Suk;Park, Chan-Woong
    • The Korean Journal of Pharmacology
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    • v.21 no.2
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    • pp.79-89
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    • 1985
  • Mechanism of calcium transport inhibition of cardiac sarcoplasmic reticulum (SR) by oxygen free radicals was examined. Effects of oxygen free radicals generated by xanthine/xanthine oxidase (X/XO) system on isolated porcine ventricle SR were studied with respect to its calcium binding, lipid peroxidation, SH-group content and alteration of membrane protein components. The results are as follows. 1) Calcium binding of isolated SR was markedly inhibited by X/XO. 2) During the incubation of sarcoplasmic reticulum with xanthine/xanthine oxidase, there were marked inclose in lipid peroxidation and reduction of SH-group content. 3) An antioxidant, p-phenylenediamine effectively prevented the lipid peroxidation but partially prevented the calcium binding inhibition of X/XO treated SR. 4) The reduction of SH-group content of SR treated with X/XO was partially prevented by p-phenylendiamine. 5) When modifying SH-group of SR by treatment with DTNB, the inhibition of calcium binding activity was partially prevented. 6) On gel-permeation chromatography of X/XO-treated sarcoplasmic reticulum, there was an increase of small molecular weight products, probably protein degradation products. 7) Semicarbazide, which prevents the cross-linking reaction of protein components, did not affect the calcium binding inhibition of X/XO-treated SR. From these results, it is suggested that the inhibition of calcium binding of SR by oxygen free radicals results from the consequence of multiple changes of SR components, which are lipid peroxidation, SH-group oxidation and degradation of protein components.

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