0
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Inactivation kinetics of peroxidase and polyphenol oxidase in peach juice treated with gaseous ozone

      Read this article at

      ScienceOpenPublisher
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The effectiveness of gaseous ozone for inactivating peroxidase ( POD) and polyphenoloxidase ( PPO) in peach juice was investigated. The suitability of first‐order and Weibull models to describe inactivation kinetics was also analysed. Peach juice was exposed to ozone (0.11 and 0.20 mg O 3 min −1  mL −1) in a bubble column up to 12 min at 20 ± 1 °C. Enzyme activities were reduced due to treatments. The magnitude of the inactivation increased with ozone level and exposure time. Reductions in activity after 12 min of treatment ranged between 99.5% and 99.8% for POD and between 93.9% and 97.3% for PPO, depending on ozone concentration. Inactivation curves were successfully fitted with the first‐order and Weibull models; although, based on the root‐mean‐square error, the corrected Akaike and the Bayesian Schwarz criterion, the Weibull model showed stronger capability in all cases.

          Related collections

          Most cited references51

          • Record: found
          • Abstract: not found
          • Book: not found

          Experimental Design and Data Analysis for Biologists

            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Protein oxidation: basic principles and implications for meat quality.

            The involvement of oxidized proteins to the development of biological diseases has been studied for a few decades, but the effects and the mechanisms of protein oxidation in food systems are largely unknown. Protein oxidation is defined as the covalent modification of a protein induced either by the direct reactions with reactive oxygen species (ROS) or indirect reactions with secondary by-products of oxidative stress. ROS can cause oxidation in both amino acid side chains and protein backbones, resulting in protein fragmentation or protein-protein cross-linkages. Although all amino acids can be modified by ROS, cysteine, and methionine that are the most susceptible to oxidative changes due to high reaction susceptibility of the sulfur group in those amino acids. Oxidative modifications of proteins can change their physical and chemical properties, including conformation, structure, solubility, susceptibility to proteolysis, and enzyme activities. These modifications can be involved in the regulation of fresh meat quality and influence the processing properties of meat products. Oxidative stress occurs when the formation of oxidants exceeds the ability of antioxidant systems to remove the ROS in organisms. Increased levels of protein oxidation have been associated with various biological consequences, including diseases and aging, in humans and other animal species. The basic principles and products of protein oxidation and the implications of protein oxidation in food systems, especially in meat, are discussed in this review.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: found
              Is Open Access

              Protein oxidation and peroxidation

              Proteins are major targets for radicals and two-electron oxidants in biological systems due to their abundance and high rate constants for reaction. With highly reactive radicals damage occurs at multiple side-chain and backbone sites. Less reactive species show greater selectivity with regard to the residues targeted and their spatial location. Modification can result in increased side-chain hydrophilicity, side-chain and backbone fragmentation, aggregation via covalent cross-linking or hydrophobic interactions, protein unfolding and altered conformation, altered interactions with biological partners and modified turnover. In the presence of O2, high yields of peroxyl radicals and peroxides (protein peroxidation) are formed; the latter account for up to 70% of the initial oxidant flux. Protein peroxides can oxidize both proteins and other targets. One-electron reduction results in additional radicals and chain reactions with alcohols and carbonyls as major products; the latter are commonly used markers of protein damage. Direct oxidation of cysteine (and less commonly) methionine residues is a major reaction; this is typically faster than with H2O2, and results in altered protein activity and function. Unlike H2O2, which is rapidly removed by protective enzymes, protein peroxides are only slowly removed, and catabolism is a major fate. Although turnover of modified proteins by proteasomal and lysosomal enzymes, and other proteases (e.g. mitochondrial Lon), can be efficient, protein hydroperoxides inhibit these pathways and this may contribute to the accumulation of modified proteins in cells. Available evidence supports an association between protein oxidation and multiple human pathologies, but whether this link is causal remains to be established.
                Bookmark

                Author and article information

                Contributors
                (View ORCID Profile)
                Journal
                International Journal of Food Science & Technology
                Int J of Food Sci Tech
                Wiley
                0950-5423
                1365-2621
                February 2018
                September 15 2017
                February 2018
                : 53
                : 2
                : 347-355
                Affiliations
                [1 ] Departamento de Industrias Facultad de Ciencias Exactas y Naturales Universidad de Buenos Aires Intendente Güiraldes, 2160 C.A.B.A C1428EGA Argentina
                [2 ] Consejo Nacional de Investigaciones Científicas y Técnicas Buenos Aires Argentina
                [3 ] Departamento de IngenieríaQuímica y Alimentos Facultad de Ingeniería Universidad Nacional de Mar del Plata Juan B. Justo 4302 Mar del Plata B7608FDQ Argentina
                Article
                10.1111/ijfs.13591
                38af380c-1a03-482e-81d7-ccb71a111d17
                © 2018

                http://onlinelibrary.wiley.com/termsAndConditions#vor

                History

                Comments

                Comment on this article