2019
DOI: 10.3390/molecules24203783
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Succinylation Improves the Thermal Stability of Egg White Proteins

Abstract: Succinylation can improve the thermal stability of various proteins. In this study, succinylated egg white protein (SEWP) samples with different succinylation degrees were prepared by adding various succinic anhydride additives to egg white protein (EWP). The thermal stability of SEWP and the conformational structure under various succinylation degrees were investigated. With the increase in succinylation degree, the turbidity of heated SEWP solution (90 °C for 30 min) markedly declined. The heated SEWP soluti… Show more

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Cited by 21 publications
(2 citation statements)
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“…SMC1-SG produced by the NTG mutant strain SMC1 showed no changes in structure, activity, or functions, according to FT-IR, 1 H NMR peak analysis, and GPC data. However, SMC1-SG showed higher thermostability than that of SG, which could be explained by the high succinylation of SMC1-SG [ 46 ].…”
Section: Resultsmentioning
confidence: 99%
“…SMC1-SG produced by the NTG mutant strain SMC1 showed no changes in structure, activity, or functions, according to FT-IR, 1 H NMR peak analysis, and GPC data. However, SMC1-SG showed higher thermostability than that of SG, which could be explained by the high succinylation of SMC1-SG [ 46 ].…”
Section: Resultsmentioning
confidence: 99%
“…Succinic anhydride acylated EY could form a denser gel network, enhance the water‐holding capacity of EY gels, and significantly increase the hardness of EY gels (Ren et al., 2020). The thermal stability of succinic anhydride‐acylated EWP was reported to be improved (He et al., 2019), which affected the formation of EWP thermally induced gels. In contrast, the thermal stability of EWP acetylated with acetic anhydride was decreased, which facilitated the formation of EWP gels (Ball & Winn, 1982).…”
Section: Modification Of Egg Protein Gelmentioning
confidence: 99%