Cloning and some properties of Japanese pear (<i>Pyrus pyrifolia</i>) polyphenol oxidase, and changes in browning potential during fruit maturation

Nishimura, Mika; Fukuda, Chieko; Murata, Masatsune; Homma, Seiichi

doi:10.1002/jsfa.1518

Cited by 20 publications

(9 citation statements)

References 31 publications

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“…The distribution of PPOs in apple and Japanese pear fruits appeared to be spatially different: mainly localized around the core for apple and throughout the fruit for Japanese pear [16]. The deduced amino acid sequence of trembling aspen PPO shows particularly significant identity with those from the woody plants (hybrid poplar, apple, apricot and grape).…”

Section: Polyphenol Oxidase (Ppo) and Ppo Genesmentioning

confidence: 95%

Functional Analysis of Polyphenol Oxidases by Antisense/Sense Technology

2007

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Polyphenol oxidases (PPOs) catalyze the oxidation of phenolics to quinones, the secondary reactions of which lead to oxidative browning and postharvest losses of many fruits and vegetables. PPOs are ubiquitous in angiosperms, are inducible by both biotic and abiotic stresses, and have been implicated in several physiological processes including plant defense against pathogens and insects, the Mehler reaction, photoreduction of molecular oxygen by PSI, regulation of plastidic oxygen levels, aurone biosynthesis and the phenylpropanoid pathway. Here we review experiments in which the roles of PPO in disease and insect resistance as well as in the Mehler reaction were investigated using transgenic tomato (Lycopersicon esculentum) plants with modified PPO expression levels (suppressed PPO and overexpressing PPO). These transgenic plants showed normal growth, development and reproduction under laboratory, growth chamber and greenhouse conditions. Antisense PPO expression dramatically increased susceptibility while PPO overexpression increased resistance of tomato plants to Pseudomonas syringae. Similarly, PPO-overexpressing transgenic plants showed an increase in resistance to various insects, including common cutworm (Spodoptera litura (F.)), cotton bollworm (Helicoverpa armigera (Hübner)) and beet army worm (Spodoptera exigua (Hübner)), whereas larvae feeding on plants with suppressed PPO activity had higher larval growth rates and Molecules 2007, 12 1570 consumed more foliage. Similar increases in weight gain, foliage consumption, and survival were also observed with Colorado potato beetles (Leptinotarsa decemlineata (Say)) feeding on antisense PPO transgenic tomatoes. The putative defensive mechanisms conferred by PPO and its interaction with other defense proteins are discussed. In addition, transgenic plants with suppressed PPO exhibited more favorable water relations and decreased photoinhibition compared to nontransformed controls and transgenic plants overexpressing PPO, suggesting that PPO may have a role in the development of plant water stress and potential for photoinhibition and photooxidative damage that may be unrelated to any effects on the Mehler reaction. These results substantiate the defensive role of PPO and suggest that manipulation of PPO activity in specific tissues has the potential to provide broad-spectrum resistance simultaneously to both disease and insect pests, however, effects of PPO on postharvest quality as well as water stress physiology should also be considered. In addition to the functional analysis of tomato PPO, the application of antisense/sense technology to decipher the functions of PPO in other plant species as well as for commercial uses are discussed.

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Section: Polyphenol Oxidase (Ppo) and Ppo Genesmentioning

confidence: 95%

Functional Analysis of Polyphenol Oxidases by Antisense/Sense Technology

2007

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“…The molecular mass of this mature PPO was calculated to be about 57 kDa. Similarity analysis of three-dimensional structure suggested that this PPO had a unique shielding region on the C-terminal side like aurone synthase, a type of PPO (Moritole et al, 2016), although PPO is usually active without limited proteolysis of the C-terminal side (Hunt et al, 1993;Haruta et al, 1998； Tsurutani et al, 2002Nishimura et al, 2003). A plausible structure of an active mung bean PPO after a transit peptide and a shielding region on the C-terminal side were removed was depicted using Swiss-Model Workspace (Arnold et al, 2006) and an active grape PPO (Virador et al, 2010) as shown in Fig.…”

Section: Resultsmentioning

confidence: 96%

“…We will need to examine whether the bands at 47 kDa and 31 kDa were the mature PPO (calculated to be 57 kDa) and the active PPO (calculated to be 38 kDa), respectively. In general, C-terminal cleavage is not required for plant PPOs to be activated (Hunt et al, 1993;Haruta et al, 1998； Tsurutani et al, 2002Nishimura et al, 2003). This unique proteolysis of mung bean PPO may become a new target for regulating the browning of mung bean sprouts, Fig.…”

Section: Ppo Expression During Cold Storage Of Mung Bean Sproutmentioning

confidence: 97%

Enzymatic Browning and Polyphenol Oxidase of Mung Bean Sprout during Cold Storage

Kogo

Sameshima

Ukena

et al. 2018

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Mung bean sprouts turn brown during cold storage. Here, we cloned polyphenol oxidase (PPO) mRNA, and then examined its expression and active form to clarify the mechanism of this browning. A PPO cDNA encoding 592 amino acids showed high homology to PPO genes of Fabaceae plants and had highly conserved motifs, including the active site and transit peptide to the plastid thylakoid. Expression of PPO mRNA was almost constant. The translated PPO protein was considered to migrate into the thylakoid, but the active PPO was mainly present in the cytosol or soluble fraction, and its molecular mass was 31 kDa, smaller than the translated protein. The membrane structure of mung bean sprouts is heavily disrupted during cold storage. These results showed that PPO transported into the thylakoid is solubilized and decomposed to its active form, which oxidizes phenolic compounds in the cytosol to turn sprouts brown during cold storage.

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“…Enzymatic methods for the synthesis of benzotropolone derivatives by the use of polyphenol oxidase or peroxidase are known; therefore, we also performed the enzymatic synthesis of goupiolone A ( 1 ). An aqueous solution of catechol ( 3 ) and ethyl gallate ( 4 ) was treated with a Japanese pear ( Pyrus pyrifolia ) fruit homogenate, which has strong polyphenol oxidase activity, to afford goupiolone A ( 1 ; 71 %) along with 5 (0.24 %) (Scheme b). This relatively high yield of 1 is attributed to the substrate specificity of polyphenol oxidase for 3 .…”

Section: Methodsmentioning

confidence: 99%

Structural Revision and Biomimetic Synthesis of Goupiolone B

et al. 2017

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Goupiolones A and B are unique phenolic compounds with significant DNA-damaging activity. In this study, the structure of goupiolone B was revised on the basis of DFT calculations of the 13 C NMR chemical shifts and biosynthetic considerations. The dibenzobicyclo[3.2.2]nonane skeleton of the revised structure suggested that goupiolone B was produced by oxidative coupling between catechol and goupiolone A, which was strongly supported by this biomimetic synthesis. Furthermore, the racemization of goupiolone B was observed during the examination for the chiral separation of its racemic mixture. A plausible racemization mechanism involving α-ketol rearrangement was also proposed.

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Cloning and some properties of Japanese pear (Pyrus pyrifolia) polyphenol oxidase, and changes in browning potential during fruit maturation

Cited by 20 publications

References 31 publications

Functional Analysis of Polyphenol Oxidases by Antisense/Sense Technology

Functional Analysis of Polyphenol Oxidases by Antisense/Sense Technology

Enzymatic Browning and Polyphenol Oxidase of Mung Bean Sprout during Cold Storage

Structural Revision and Biomimetic Synthesis of Goupiolone B

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