• Title, Summary, Keyword: polyphenol oxidase

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Inhibitory Effect of Pine Needle(Pinus densiflora S.) Extract on Potato Polyphenol Oxidase (감자 polyphenol oxidase에 대한 솔잎 추출물의 저해효과)

  • Lee, Min-Kyung
    • Journal of Life Science
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    • v.16 no.5
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    • pp.866-869
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    • 2006
  • The inhibitory effect of pine needle (Pinus densiflora S.) on potato polyphenol oxidase (PPO) was investigated. The addition of the pine needle extract exhibited a higher inhibitory effect on the potato polyphenol oxidase activity than that of the citric acid or potassium sorbate. The enzyme activity was strongly inhibited in a pH range of 7.0-8.0. When the incubation time of reaction mixture was increased, the potato polyphenol oxidase activity was markedly inhibited. The pine needle extract inhibited the potato polyphenol oxidase non-competitively. And also the pine needle extract subjected to a heat treatment at $100^{\circ}C$ for 10 min or to an acid treatment at pH 2.0, 3.0, and 4.0 for 3 hours still retained inhibitory effect on potato polyphenol oxidase.

Purification of the Glycosylated Polyphenol Oxidase from Potato Tuber

  • Kwon, Do-Yoon;Kim, Woo-Yeon
    • BMB Reports
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    • v.29 no.2
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    • pp.163-168
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    • 1996
  • Glycosylated polyphenol oxidase was purified from potato tuber using ammonium sulfate fractionation, Sephadex G-100, and concanavalin A Sepharose column chromatography. Two or three types of polyphenol oxidase were separated on concanavalin A Sepharose. Type I and II polyphenol oxidases did not bind to concanavalin A Sepharose. Type I seemed to be an aggregated form of polyphenol oxidase. Type III polyphenol oxidase, which is presumed to be glycosylated because it was bound to concanavalin A Sepharose and eluted with $\alpha$-D-methyl glucopyranoside, was further purified by chromatography on Econo-Pac Q and Superose 12. Glycosylated polyphenol oxidase was purified 130-fold from the dissolved ammonium sulfate pellet resulting in about $6\;{\mu}g$ of the enzyme from 100 g of potato tuber periderm. The molecular weight of the glycosylated enzyme determined by SDS-polyacrylamide gel electrophoresis was about 64,000. Optimum temperature and pH of both II and type III potato polyphenol oxidases were $20^{\circ}C$ and pH 7.0, respectively. Glycosylated form of polyphenol oxidase (type III) preferred catechol to catechin as a substrate, whereas type II enzyme showed the reverse substrate preference.

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Properties of Extracellular Polyphenol Oxidase Isolated from Lentinus edodes JA01 (Lentinus edodes JA01에서 분리한 세포외 polyphenol oxidase의 부분적 성질에 관하여)

  • 신광수;김규중;홍순우;하영칠
    • Korean Journal of Microbiology
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    • v.24 no.2
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    • pp.141-146
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    • 1986
  • To find the role of polyphenol oxidase in lignin biodegradation, chracteristics of extracellular polyphenol oxidase activity from Lentinus edodes JA01 was investigated. Polyphenol oxidase had its optimum activity at pH 4.5 and $45^{\circ}C$ respectively. Also, the enzyme was very unstable in various pHs and comparatively heat stable up to $60^{\circ}C$. In $lignosulfonate-NH_4$ salts medium, the growth rate of L.edodes JA 01 was relatively slow and polyphenol oxidase activity appeared 2 and 14 days after inoculation. No significant relationships were found between polyphenol oxidase activity and the amounts of lignosulfonate present in the culture medium.

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The Inhibitory Effect of Polyphenol Oxidase on Polyphenol-Induced DNA Damage of Bacillus subtilis (고초균에서 폴리페놀로 유도된 DNA 손상에 대한 폴리페놀산화효소의 억제효과)

  • Kim An Keun;Kim Yoo Kyung;Kang Young-Sook
    • YAKHAK HOEJI
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    • v.49 no.4
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    • pp.330-334
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    • 2005
  • Antimutagenic activity of the enzymatic browning reaction products (EBRPs) was investigated by using the spore rec-assay with Bacillus subtilis strains H17 $(rec^+)\;and\;M45 (rec^-)$. The EBRPs tested were prepared from the reactions of five different kinds of polyphenols with polyphenol oxidase isolated from the leaves Perilla frutescens. In the spore rec-assay, most of the polyphenolic compounds tested showed positive, whereas only their tested compound showed negative respectively. In addition of polyphenol oxidase inhibitors such as cysteine, glutathione and ascorbic acid to the reaction mixtures consisted with the polyphenol oxidase and polyphenols, the mutagenic effects were increased in the spore recassay. These results show that the activity of polyphenol oxidase may play an important role in the reduction of mutagenicity of polyphenols.

Inhibition of Polyphenol Oxidase and Peach Juice Browning by Onion Extract

  • Kim, Choon-Young;Kim, Mi-Jeong;Lee, Min-Young;Park, In-Shik
    • Food Science and Biotechnology
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    • v.16 no.3
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    • pp.421-425
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    • 2007
  • The inhibitory effect of onion extract on polyphenol oxidase (PPO) and browning of peach juice was investigated. Various reducing agents such as L-ascorbic acid, L-cysteine, dithiothreitol, glutathione, and sodium pyrosulfite strongly inhibited polyphenol oxidase extracted from peach. The enzyme was also inhibited by addition of water extract of onion. Regardless of substrates used, the addition of heated onion extract exhibited stronger inhibitory effect on peach polyphenol oxidase activity than that of the fresh one. The inhibitory effect of onion extract was dependent on heating temperature and time. The onion extract inhibited the peach polyphenol oxidase non-competitively. The heating of onion extract in the presence of glucose, glycine stimulated the inhibitory effect of the onion extract, which suggests non-enzymatic browning products produced during heating might be responsible for the stronger inhibitory action of the heated onion extract. The retardation of peach juice browning by onion extract seems to be caused by inhibition of peach PPO.

Partial Purification and Some Properties of Polyphenol Oxidase from Aster scaber (참취로부터 추출한 Polyphenol Oxidase의 부분정제 및 성질)

  • 함승시;홍은희;이상영;박귀근;오무라히라히사
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.20 no.3
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    • pp.241-245
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    • 1991
  • A polyphenol oxidase from the crude extract of Aster scaber was partially purified by (NH4)2 SO4 precipitation and subsequent Sephadex G-150 chromatography. The final preparation showed five peaks of enzyme activity. Optimum pH and temperature for the activity of polyphenol oxidase were 7.0 and $30^{\circ}C$, respectively. Enzyme activity was stable at $40^{\circ}C$ for 5min in pH 7.0 reaction mixture but ceased completely at $60^{\circ}C$ for 30min and $70^{\circ}C$ for 5min at pH 7.0. The olyphenol oxidase has good activity acid but was inactive on DL-depa. The apparent Km for catechol was about 17.6mM.

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Characteristics and Inhibition of Polyphenol Oxidase from Fuji Apples (후지 사과 Polyphenol Oxidase의 특성 및 활성억제)

  • Choi, Eon-Ho;Jung, Dong-Sun;Cho, Nam-Sook;Shim, Young-Hyun
    • Applied Biological Chemistry
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    • v.30 no.3
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    • pp.278-284
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    • 1987
  • As a basic research for inhibition of enzymatic browning of apples during dehydration or processing, polyphenol oxidase was extracted from Fuji apples to investigate heat inactivation, chemical inhibition and other properties. Polyphenol oxidase showed the highest activity at $20^{\circ}C$ and pH 5.5 with catechol as substrate, and the Michaelis constant of 0.14 M under the same condition of substrate and pH. The thermal inactivation followed pseudo first-order kinetics to have activation energy of 23.0 kcal/mol and z value of $19.7^{\circ}C$. As for substrate specificity the polyphenol oxidase showed high affinity toward the o-diphenolic compounds, particularly chlorogenic acid. Neither the m- and p-dihydroxy phenols nor monophenols were attacked. Browning by polyphenol oxidase was completely inhibited at the concentrations of 10mM for potassiummetasulfite and thiourea and 1mM for L-cysteine, ascorbic acid and sodium diethyldithiocarbamate.

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Purification and some properties of polyphenol oxidase from Spuriopimpinella bracycarpa (참나물로부터 추출한 polyphenol oxidase의 부분정제 및 성질)

  • Ham, Seung-Shi;Hong, Eun-Hee;Lee, Sang-Young;Park, Gwi-Gun;Omura, Hirohisa
    • Applied Biological Chemistry
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    • v.34 no.1
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    • pp.49-53
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    • 1991
  • Three polyphenol oxidase(polyphenol oxidase I, II and III ) were isolated from the crude extract of a Spuriopimpinella bracycarpa by $(NH_4)_2SO_4$ precipitation and subsequent Sephadex G-150 chromatography. The final preparation thus obtained showed three peaks of enzyme activity. Optimum pH and temperature for the activity of polyphenol oxidase were 7.5 and $30^{\circ}C$, respectively. The enzyme was completely inactivated when i4 was treated at$70^{\circ}C$ for 30min and at $80^{\circ}C$ for 5min at pH 6.5. The enzyme was partially inactivated by ascorbic acid, glutathione and potassium cyanide (0.1mM), and was completely inhibited by L-cysteine, ascorbic acid, glutathione and potassium cyanide(0.5 and 1.0mM). The enzyme has good activity on catechol and 3,4-dihydroxytoluene but was strongly inactivated on pyrogallol, dopamine and DL-dopa. The Michaelis cons4ant of the enzyme was 86.5mM with catechol as a substrate.

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Physio-chemical studies on the seed-browning in mature green peppers stored at low-temperature (Part 2) -Changes in enzymatic activity with the seed-browning effect- (녹숙(綠熟)고추의 저온저장(低溫貯藏)에 따른 종자갈변(種子褐變)에 관(關)한 생리화학적연구(生理化學的硏究) -제 2 보(第 2 報) 종자갈변(種子褐變)에 따른 효소활성(酵素活性)의 변화(變化)-)

  • Lee, Sung-Woo
    • Korean Journal of Food Science and Technology
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    • v.3 no.1
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    • pp.37-43
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    • 1971
  • (1) Relatively active polyphenol oxidase influence was seen at $0{\circ}C$, and the optimal pH level for the enzyme from the seeds of a small type sweet pepper Zairaisisi is 6.5. (2) The starting stage of the brown coloration with low-temperature injuries showed a strong activity of polyphenol oxidase, and the activity drops to 0 as the entire seed became brownish. (3) The browning effect with enzyme solution of polyphenol extracts suggested that the brown coloration continues in vitro even if polyphenol oxidase activity is nil. (4) Although cytochrome oxidase activity dropped when an abnormality occurrs in electron pathways of respiration at the starting stage of the browning with low temperature injuries, there was no marked influence of it on the total respiration, indicating the fact that polyphenol oxidase can take place of terminal oxidase in the compensatory respiration process.

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Some Properties of the Polyphenol Oxidase from Potatoes (Solanum tubersum L.) and Inhibiting Effect of the Polyphenol Oxidase by Sulfites (감자 Polyphenol Oxidase의 효소학적 성질 및 아황산염에 의한 활성억제 효과)

  • Ha, Young-Duk;Lee, Mi-Ock
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.17 no.3
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    • pp.198-204
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    • 1988
  • This study was aimed at obtaining elementary data on enzymatic browning of potato and potato products and examining the inhibitory method of browning. Therefore, we extracted polyphenol oxidase from potatoes(Solanum tubersum L.), and investigates its general properties and inhibiting effects of its activity with the different concentrations of sulfites($Na_2S_2O_4,\;Na_2SO_3{\cdot}7H_2O,\;NaHSO_3$). The optimum pH and temperature of polyphenol oxidase were observed to be 6.5 and $37^{\circ}C$ respectively. The polyphenol oxidase at PH5 was very stable, and the activity of polyphenol oxidase between pH $5.0{\sim}9.0$ was estimated to be relatively high, showing $72{\sim}75%$ of its activity at pH5. The polyphenol oxidase was very stable when heated at $40^{\circ}C$ for one hour, and almost 50% of enzyme activity was decreased when heated at $70^{\circ}C$ for twelve minutes. At 0.1mM concentrating of sulfites the relative activity of polyphenol oxidase was 98% in all the three cases of sulfites. Thus sulfites at 0.1mM concentration was found to have little inhibiting effect on polyphenol oxidase activity. At 1mM concentration of sulfites $NaHSO_3$ showed the lowest 36% relative activity among the three. At 5mM concentration of sulfites, the relative activity of $Na_2SO_3{\cdot}7H_2O$ was the lowest 14%.

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