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      Effect of slurry ice during storage on myofibrillar protein of Pseudosciaena crocea

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          Abstract

          In order to explore the effect of slurry ice on myofibrillar protein of Pseudosciaena crocea, the changes in myofibrillar protein and muscle microstructure during storage were studied with crushed ice as a control. During the storage period, the rate of decrease in myofibrillar protein content, Ca 2+‐ATPase activity, and total sulfhydryl groups in the slurry ice group was lower than in the control group ( p < .05). There was a significant linear correlation between the hydrophobicity and the storage time ( R crushed ice (4℃) = 0.9881, R slurry ice (4℃) = 0.9878, R slurry ice (−1℃) = 0.9674), and trichloroacetic acid (TCA) soluble peptide content was lower than in the control group at the same time. Slurry ice (−1℃) was optimal in maintaining protein content in P. crocea; the arrangement of myofibrils in P. crocea treated by slurry ice was compact and the gaps were small. Slurry ice can delay the denaturation and degradation of fish myofibrillar protein and maintain its quality.

          Abstract

          Slurry ice can delay the denaturation and degradation of fish myofibrillar protein. Slurry ice (−1℃) is the best one to keep protein of Pseudosciaena crocea. There was a linear correlation between the hydrophobicity and the storage time.

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          Tissue sulfhydryl groups

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            Protein carbonyls in meat systems: a review.

            Protein oxidation (P-OX) is an innovative topic of increasing interest among meat researchers. Carbonylation is generally recognized as one of the most remarkable chemical modifications in oxidized proteins. In fact, the quantification of protein carbonyls by the dinitrophenylhydrazine (DNPH) method is the most common procedure for assessing P-OX in meat systems. Numerous studies have investigated the occurrence of protein carbonylation right after slaughter and during subsequent processing and cold storage of meat. However, the significance of protein carbonylation in meat systems is still poorly understood. Beyond their role as markers of protein oxidation, specific protein carbonyls such as α-aminoadipic and γ-glutamic semialdehydes (AAS and GGS, respectively) are active compounds that may be implicated in several chemical reactions with relevant consequences on meat quality. The formation of protein carbonyls from particular amino acid side chains contribute to impair the conformation of myofibrillar proteins leading to denaturation and loss of functionality. Recent studies also highlight the potential impact of specific protein carbonyls in particular meat quality traits such as water-holding capacity (WHC), texture, flavor and its nutritional value. As a truly emerging topic, the results from current studies provide grounds from the development of further investigations. The present paper reviews the current knowledge on the mechanisms and consequences of protein carbonylation in meat systems and aims to encourage meat researchers to accomplish further investigations on this fascinating research topic.
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              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.
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                Author and article information

                Contributors
                yuan2007019@163.com
                Journal
                Food Sci Nutr
                Food Sci Nutr
                10.1002/(ISSN)2048-7177
                FSN3
                Food Science & Nutrition
                John Wiley and Sons Inc. (Hoboken )
                2048-7177
                04 June 2021
                July 2021
                : 9
                : 7 ( doiID: 10.1002/fsn3.v9.7 )
                : 3806-3814
                Affiliations
                [ 1 ] College of Biological and Environmental Sciences Zhejiang Wanli University Ningbo P.R. China
                [ 2 ] Department of Genetics, Bioinformatics and Computational Biology Virginia Polytechnic Institute and State University Blacksburg VA USA
                Author notes
                [*] [* ] Correspondence

                Yongjun Yuan, College of Biological and Environmental Sciences, Zhejiang Wanli University, 315100 Ningbo, P.R. China.

                Email: yuan2007019@ 123456163.com

                Author information
                https://orcid.org/0000-0002-5047-6934
                Article
                FSN32355
                10.1002/fsn3.2355
                8269672
                34262738
                e2f8442a-206b-4885-847c-3d85ea2e1ecf
                © 2021 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 30 April 2021
                : 11 January 2021
                : 08 May 2021
                Page count
                Figures: 7, Tables: 0, Pages: 9, Words: 5728
                Funding
                Funded by: Fishery science and technology project of Ningbo Marine and Fisheries Bureau of China
                Award ID: NITY20170328062
                Funded by: Zhejiang Provincial Natural Science Foundation of China
                Award ID: LY17C010001
                Funded by: Ningbo Natural Science Foundation of China , doi 10.13039/100007834;
                Award ID: 2017A610287
                Funded by: College Student Technological Creativity Program of Zhejiang Province in 2021
                Funded by: Zhejiang Provincial Top Discipline of Biological Engineering (Level A)
                Award ID: ZS2016003
                Categories
                Original Research
                Original Research
                Custom metadata
                2.0
                July 2021
                Converter:WILEY_ML3GV2_TO_JATSPMC version:6.0.4 mode:remove_FC converted:09.07.2021

                crushed ice,fish refrigeration,myofibrillar protein,pseudosciaena crocea,slurry ice

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