Thermostabilities of plant phenol oxidase and peroxidase determining the technology of their use in the food industry

Mchedlishvili, N. I.; Omiadze, N. T.; Gulua, L.; Sadunishvili, Tinatin; Zamtaradze, R. K.; Abutidze, M. O.; Bendeliani, E. G.; Kvesitadze, G.

doi:10.1007/s10438-005-0024-6

Cited by 8 publications

(4 citation statements)

References 17 publications

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“…Very early work suggested that ''polyatomic phenol oxidase'' activity in walnut hulls produced a germicidal fluid that could inhibit bacterial growth (Cook et al, 1911). More recent studies have described the thermostability and basic biochemical properties of PPO activity in walnut hull extracts (Mchedlishvili et al, 2005;Piffaut and Metche, 1991). Overall, however, very little is known about the biochemistry and molecular biology of PPOs in walnut.…”

mentioning

confidence: 99%

Characterization of Polyphenol Oxidase from Walnut

Escobar¹,

Shilling²,

Higgins³

et al. 2008

J. Amer. Soc. Hort. Sci.

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The enzyme polyphenol oxidase (PPO) is nearly ubiquitous in Kingdom Plantae and catalyzes the oxidation of phenolic compounds into highly reactive quinones. Although the functional importance of PPO in plants remains uncertain, a putative antipathogen role for walnut (Juglans regia) PPO was posited as early as 1911. However, despite the rich diversity of phenolics present in walnut leaves and hulls, walnut PPO has been little studied since the early 1900s. We cloned a PPO-encoding gene from a walnut pistillate flower cDNA library and designated the gene jrPPO1. Genomic Southern analysis demonstrated that jrPPO1 is the sole PPO gene in walnut. Transgenic tobacco (Nicotiana tabacum) plants expressing jrPPO1 display greater than 10-fold increases in leaf PPO activity compared with wild-type tobacco, demonstrating that jrPPO1 encodes a functional enzyme. The jrPPO1 protein is expressed primarily in the leaves, hulls, and flowers of walnut trees and is not regulated by wounding or methyl jasmonate. To examine whether walnut PPO could affect pathogen resistance, tobacco plants expressing jrPPO1 were challenged with Pseudomonas syringae pv. tabaci. Based on both symptom development and quantitative analyses of bacterial growth in planta, the PPO-expressing plants did not display increased resistance to this pathogen. Leaf extract browning assays indicated that tobacco leaves lack the endogenous phenolic substrates required for significant jrPPO1 activity and quinone production in planta.

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mentioning

confidence: 99%

Characterization of Polyphenol Oxidase from Walnut

Escobar¹,

Shilling²,

Higgins³

et al. 2008

J. Amer. Soc. Hort. Sci.

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“…Recent proteomics studies confirm that malting barley cultivar variation in peroxidase isozyme spatio-temporal profiles might affect the colour and clarity of the wort, and probably the beer, and play a role in the metabolism of oxygen during mashing 94 . Different ways to control the undesirable activity of peroxidases during brewing have been suggested 109,126 .…”

Section: Beer Colloidal Stabilitymentioning

confidence: 99%

A Review: The Role of Barley Seed Pathogenesis-Related Proteins (PRs) in Beer Production

Gorjanović

2010

Journal of the Institute of Brewing

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Pathogenesis-related proteins (PRs) are involved in the protection of dormant and germinating cereal seeds against pathogenic microorganisms and pests. Moreover, barley grain PRs have considerable technological importance in the brewing of beer. The compact structure of PRs allows them to survive the hostile conditions of the extracellular compartments, where they are usually localized, and enables the endurance of certain classes of PRs during the harsh conditions of the technological steps of beer production. Beer proteome maps reveal a dominant presence of PRs and facilitate association between particular proteins and specific beer quality traits. Current knowledge on the influence of PRs on the various aspects of beer quality has been summarized in this review.

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“…Cultivar variation in barley seed peroxidase isozyme spatio-temporal profiles might affect beer quality 8,9,177 . Beer turbidity during storage could perhaps be prevented using natural inhibitors of these enzymes 212 . Seed-specific peroxidases from cereals appear to be important allergens in hypersensitive diseases associated with the manipulation of flour 19,292 .…”

Section: Peroxidases (Pr-9)mentioning

confidence: 99%

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

Gorjanović

2009

Journal of the Institute of Brewing

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The mature barley seed proteome is dominated by proteins involved in stress responses, including the Pathogenesis-Related proteins (PRs). PRs are currently classified into 17 families. The biochemistry of the PRs families, whose members are constitutively present in barley seed, is surveyed in this paper. These proteins are assumed to protect dormant and germinating seeds against pathogenic microorganisms and pests. The current knowledge on PRs structural and functional properties is summarized in an attempt to illustrate their importance in barley seed innate resistance. At the same time, a platform to understand PRs technological function in cereal foods and in beverage processing and quality is provided.

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Thermostabilities of plant phenol oxidase and peroxidase determining the technology of their use in the food industry

Cited by 8 publications

References 17 publications

Characterization of Polyphenol Oxidase from Walnut

Characterization of Polyphenol Oxidase from Walnut

A Review: The Role of Barley Seed Pathogenesis-Related Proteins (PRs) in Beer Production

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

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