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      Effects of temperature on quality of preserved eggs during storage

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          Abstract

          The effects of storage temperature (4°C, 25°C, and 35°C) on sensory quality, physicochemical properties, texture, molecular forces, flavor, and microbial indexes of preserved eggs were studied. The results showed that the sensory quality, weight loss rate, pH, and color of preserved eggs were significantly different at different storage temperatures ( P < 0.05). Compared with high temperature and normal temperature storage, low temperature storage reduced weight loss rate by 55.15 and 64.1%, respectively, improved the sensory score ( P < 0.05), inhibited the reduction of pH and the increase of total volatile base nitrogen ( P < 0.05), and decreased the change of color ( P < 0.05). During storage, there was no difference in the springiness of preserved egg white stored at different temperatures ( P > 0.05). Hardness and chewiness at 3 different temperatures increased first and then decreased, and low temperature significantly inhibited the progress of these changes to a certain extent ( P < 0.05). The content of ionic bond in egg white first decreased and then increased, and content of disulfide bond increased first and then decreased. Content of ionic bond in yolk decreased all the time, and high temperature could promote this change. Whatever the temperature was, the content of free amino acids in preserved egg white and yolk increased first and then decreased, and the total content of amino acids stored at different temperatures was significantly different ( P < 0.05). The content of free fatty acids in yolk decreased. At the end of storage, no microorganisms were detected in 3 temperatures during the storage period of 84 D. The results showed that low temperature storage is more conducive for preservation of preserved eggs.

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          Advanced glycation endproducts in food and their effects on health.

          Advanced glycation endproducts (AGEs) form by Maillard-reactions after initial binding of aldehydes with amines or amides in heated foods or in living organisms. The mechanisms of formation may include ionic as well as oxidative and radical pathways. The reactions may proceed within proteins to form high-molecular weight (HMW) AGEs or among small molecules to form low-molecular weight (LMW) AGEs. All free amino acids form AGEs, but lysine or arginine side chains dominate AGE formation within proteins. The analysis of AGEs in foods and body fluids is most often performed by ELISA or LC-MS; however, none of the methodologies cover all HMW and LMW AGEs. Most research is, therefore, carried out using 'representative' AGE compounds, most often N(ε)-carboxymethyl-lysine (CML). Only LMW AGEs, including peptide-bound forms, and carbonyls may be absorbed from the gut and contribute to the body burden of AGEs. Some AGEs interact with specific pro- or anti-inflammatory receptors. Most studies on the biological effects of AGEs have been carried out by administering heated foods. The pro-inflammatory and deteriorating biological effects of AGEs in these studies, therefore, need further confirmation. The current review points out several research needs in order to address important questions on AGEs in foods and health.
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            Development of simplified models for nondestructive hyperspectral imaging monitoring of TVB-N contents in cured meat during drying process

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              Protein disulfide engineering.

              Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well-defined geometric conformations, thus making them appealing candidates in protein engineering efforts. Disulfide engineering is the directed design of novel disulfide bonds into target proteins. This important biotechnological tool has achieved considerable success in a wide range of applications, yet the rules that govern the stabilizing effects of disulfide bonds are not fully characterized. Contrary to expectations, many designed disulfide bonds have resulted in decreased stability of the modified protein. We review progress in disulfide engineering, with an emphasis on the issue of stability and computational methods that facilitate engineering efforts. Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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                Author and article information

                Contributors
                Journal
                Poult Sci
                Poult Sci
                Poultry Science
                Elsevier
                0032-5791
                1525-3171
                05 March 2020
                June 2020
                05 March 2020
                : 99
                : 6
                : 3144-3157
                Affiliations
                []Engineering Research Center of Biomass Conversion, Ministry of Education, Nanchang University, Nanchang 330047, China
                []State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China
                []Jiangxi Key Laboratory of Natural Products and Functional Food, Jiangxi Agricultural University, Nanchang 330045, China
                Author notes
                Article
                S0032-5791(20)30097-3
                10.1016/j.psj.2020.01.020
                7597647
                32475451
                8fd69c30-eae3-4c13-99e8-0680b9bb5198
                © 2020 Published by Elsevier Inc. on behalf of Poultry Science Association Inc.

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                : 28 September 2019
                : 9 January 2020
                Categories
                Metabolism and Nutrition

                preserved egg,storage,temperature,quality
                preserved egg, storage, temperature, quality

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