Search results for "Catechol oxidase"
showing 10 items of 44 documents
Concentration dependent effects of commonly used pesticides on activation versus inhibition of the quince (Cydonia Oblonga) polyphenol oxidase
2009
Polyphenol oxidase (PPO) catalyzes the oxidation of o-diphenols to their respective quinones which undergo autopolymerization and form dark pigments. The interaction of PPO with various substrates and effectors remains the focus of intensive investigations due to the enzyme's key role in pigments biosynthesis including animal melanogenesis and fruit/fungi enzymatic browning. In this study, the effect of a range of commonly used pesticides on the enzyme activity has been evaluated using the purified quince (Cydonia oblonga Miller) PPO. The biochemical analysis showed that, in the presence of high pesticide concentrations, the enzyme was competitively inhibited, particularly with benomyl, car…
Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
2000
The enzymes tyrosinase, catecholoxidase and hemocyanin all share similar active sites, although their physiological functions differ. Hemocyanins serve as oxygen carrier proteins, and tyrosinases and catecholoxidases (commonly referred to as phenoloxidases in arthropods) catalyze the hydroxylation of monophenols or the oxidation of o-diphenols to o-quinones, or both. Tyrosinases are activated in vivo by limited proteolytic cleavage, which might open up substrate access to the catalytic site. It has recently been demonstrated that if hemocyanins are subjected to similar proteolytic treatments (in vitro) they also exhibit at least catecholoxidase reactivity. On the basis of their molecular st…
Tyrosinase versus Catechol Oxidase: One Asparagine Makes the Difference
2015
Tyrosinases mediate the ortho-hydroxylation and two-electron oxidation of monophenols to ortho-quinones. Catechol oxidases only catalyze the oxidation of diphenols. Although it is of significant interest, the origin of the functional discrimination between tyrosinases and catechol oxidases has been unclear. Recently, it has been postulated that a glutamate and an asparagine bind and activate a conserved water molecule towards deprotonation of monophenols. Here we demonstrate for the first time that a polyphenoloxidase, which exhibits only diphenolase activity, can be transformed to a tyrosinase by mutation to introduce an asparagine. The asparagine and a conserved glutamate are necessary to…
Full inhibition of enzymatic browning in the presence of thiol-functionalised silica nanomaterial
2018
[EN] Darkening processed fruits and vegetables is caused mainly by enzymatic browning through polyphenol oxidase (PPO) action. Accordingly, we explored the potential of four silica-based materials (MCM-41 nanometric size, MCM-41 micrometric size, UVM-7 and aerosil), non-functionalised and functionalised with thiol groups, to inhibit PPO activity in the model system and apple juice. All materials showed relevant performance when immobilising and inhibiting PPO in model systems, and support topology is a main factor for enzyme immobilisation and inhibition. Thiol-containing silica UVM7-SH showed the greatest inactivation, and similar browning values to those obtained by acidification. The enz…
Influence of the functionalisation of mesoporous silica material UVM-7 on polyphenol oxidase enzyme capture and enzymatic browning
2020
Polyphenol oxidase (PPO), also known as tyrosinase and catechol oxidase, is the enzyme responsible for enzymatic browning in foods. It causes undesirable organoleptic, nutritional and colour changes. Here, we report the preparation of five nanomaterials and a study of their ability to modulate PPO enzyme activity. The materials consist of UVM-7 supports (a mesoporous silica material) modified with diverse functional groups (i.e. amine, carboxylic acid, isocyanate, alkane and pyridine). We also studied the PPO immobilisation capability of the materials. All the materials, except the carboxylic acid functionalised one, offer high PPO loading capabilities and the immobilisation speed increases…
A new method for the cytochemical demonstration ofp-diphenol: O2 oxidoreductase (laccase)
1971
Nachweis des Enzymsp-Diphenol: O2 oxidoreductase (Laccase) in den Zellen der PilzeAspergillus fumigatus, Aureobasidium pullulans undNeurospora sitophila durch einen Azofarbstoff, der mittels Kupplung des enzymatisch gebildetenp-Chinons mitBesthorn's Hydrazon(3-Methyl-benzthiazolon(2)-hydrazon-hydrochlorid) entsteht. Als Substrat wird Hydrochinon verwendet. Der Farbstoff wird in runden, rotbraunen Granula abgelagert. Kontrollreaktionen bestatigen die Spezifitat der Reaktion.
Reactive oxygen and ethylene are involved in the regulation of regurgitant-induced responses in bean plants.
2004
Summary Application of regurgitant from Leptinotarsa decemlineata Say on wound surfaces of one wounded leaf of intact bean ( Phaseolus vulgaris L.) plants resulted in activation of ethylene biosynthesis followed by an increase of both peroxidase and polyphenol oxidase activity. The aim of the present investigation was to study the source of increased oxidative enzyme activities in regurgitant-treated bean leaves and to determine if hydrogen peroxide and ethylene biosynthesis is responsible for regurgitant-induced amplification of wound responses in bean plants. As the regurgitant contained relative high activities of both peroxidase and polyphenol oxidase, there is a possibility that increa…
Origin of the natural variation in the storage of dietary carotenoids in freshwater amphipod crustaceans
2020
16 pages; International audience; Carotenoids are diverse lipophilic natural pigments which are stored in variable amounts by animals. Given the multiple biological functions of carotenoids, such variation may have strong implications in evolutionary biology. Crustaceans such as Gammarus amphipods store large amounts of these pigments and inter-population variation occurs. While differences in parasite selective pressure have been proposed to explain this variation, the contribution of other factors such as genetic differences in the gammarid ability to assimilate and/or store pigments, and the environmental availability of carotenoids cannot be dismissed. This study investigates the relati…
POLYPHENOL OXIDASE ACTIVITY FROM THREE SICILIAN ARTICHOKE (CYNARA CARDUNCULUS L. VAR. SCOLYMUS L. (FIORI)) CULTIVARS: STUDIES AND TECHNOLOGICAL APPLI…
2010
Several papers helped with the development of more methods to control browning, or study thermal polyphenol oxidase (PPO) inactivation, but did not provide any solutions to technological process problems and food process improvement. Artichokes [ Cynara cardunculus L. var. scolymus L. (Fiori)] are susceptible to browning; this alteration could affect and reduce the suitability for its use, fresh or processed. Within this study, the catecholase and cresolase activities of PPO from three different Sicilian artichokes cultivar were characterized with regard to substrate specificity and enzyme kinetics, optimum pH and temperature, temperature and pH stability, and inhibitor test; all of the res…
Immune depression induced by acanthocephalan parasites in their intermediate crustacean host: consequences for the risk of super-infection and links …
2009
9 pages; International audience; Parasite survival in hosts mainly depends on the capacity to circumvent the host immune response. Acanthocephalan infections in gammarids are linked with decreased activity of the prophenoloxidase (ProPO) system, suggesting an active immunosuppression process. Nevertheless, experimental evidence for this hypothesis is lacking: whether these parasites affect several immune pathways is unknown and the consequences of such immune change have not been investigated. In particular, the consequences for other pathogens are not known; neither are the links with other parasite-induced manipulations of the host. Firstly, using experimental infections of Pomphorhynchus…