Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel
In order to improve the characteristics of egg white protein gel and the stability of egg white protein gel products. In this work, the changes of the texture, physicochemical properties, secondary structure and microstructure of ultrasound modified egg white protein gel (UEP) and tea polyphenols (T...
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2021
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oai:doaj.org-article:665a638e539b4ed3b7b520b2c0681dbd2021-12-04T04:33:23ZMechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel1350-417710.1016/j.ultsonch.2021.105857https://doaj.org/article/665a638e539b4ed3b7b520b2c0681dbd2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1350417721003990https://doaj.org/toc/1350-4177In order to improve the characteristics of egg white protein gel and the stability of egg white protein gel products. In this work, the changes of the texture, physicochemical properties, secondary structure and microstructure of ultrasound modified egg white protein gel (UEP) and tea polyphenols (TP) assisted ultrasound modification of egg white protein gel (TUEP) with different ultrasonic power (0–360 W) were studied. With the increase of ultrasonic power, soluble protein, surface hydrophobicity and disulfide bonds of TUEP and UEP showed an increasing trend. In particular, with the increase of ultrasonic power, the content of intramolecular β-sheets and α-helices of TUEP showed an increasing trend, and significantly improved the relaxation time and microstructure, thus enhancing TUEP gel stability. In addition, the hardness and water holding capacity (WHC) of TUEP and UEP can be increased by ultrasonic treatment, and when the ultrasonic power reached 120 W, the hardness and WHC reached the maximum. The hardness and WHC of TUEP were significantly better than that of UEP. SDS-PAGE results showed that the peptide chain of protein without being broken under ultrasonic treatment. Ultrasonic treatment can improve the gel strength of egg white protein by promoting the cross-linking of proteins to form a dense gel structure, and egg white protein gel form more disulfide bonds and a more stable gel conformation under TP assisted ultrasound. In conclusion, ultrasound and TP assisted ultrasound modification of egg white protein gel is a reliable technique, which can improve the value of egg white protein in food processing.Hui XueYonggang TuGuowen ZhangXiaojuan XinHui HuWei QiuDandan RuanYan ZhaoElsevierarticleUltrasoundEgg whiteTea polyphenolsModifyGelationChemistryQD1-999Acoustics. SoundQC221-246ENUltrasonics Sonochemistry, Vol 81, Iss , Pp 105857- (2021) |
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Ultrasound Egg white Tea polyphenols Modify Gelation Chemistry QD1-999 Acoustics. Sound QC221-246 |
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Ultrasound Egg white Tea polyphenols Modify Gelation Chemistry QD1-999 Acoustics. Sound QC221-246 Hui Xue Yonggang Tu Guowen Zhang Xiaojuan Xin Hui Hu Wei Qiu Dandan Ruan Yan Zhao Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
description |
In order to improve the characteristics of egg white protein gel and the stability of egg white protein gel products. In this work, the changes of the texture, physicochemical properties, secondary structure and microstructure of ultrasound modified egg white protein gel (UEP) and tea polyphenols (TP) assisted ultrasound modification of egg white protein gel (TUEP) with different ultrasonic power (0–360 W) were studied. With the increase of ultrasonic power, soluble protein, surface hydrophobicity and disulfide bonds of TUEP and UEP showed an increasing trend. In particular, with the increase of ultrasonic power, the content of intramolecular β-sheets and α-helices of TUEP showed an increasing trend, and significantly improved the relaxation time and microstructure, thus enhancing TUEP gel stability. In addition, the hardness and water holding capacity (WHC) of TUEP and UEP can be increased by ultrasonic treatment, and when the ultrasonic power reached 120 W, the hardness and WHC reached the maximum. The hardness and WHC of TUEP were significantly better than that of UEP. SDS-PAGE results showed that the peptide chain of protein without being broken under ultrasonic treatment. Ultrasonic treatment can improve the gel strength of egg white protein by promoting the cross-linking of proteins to form a dense gel structure, and egg white protein gel form more disulfide bonds and a more stable gel conformation under TP assisted ultrasound. In conclusion, ultrasound and TP assisted ultrasound modification of egg white protein gel is a reliable technique, which can improve the value of egg white protein in food processing. |
format |
article |
author |
Hui Xue Yonggang Tu Guowen Zhang Xiaojuan Xin Hui Hu Wei Qiu Dandan Ruan Yan Zhao |
author_facet |
Hui Xue Yonggang Tu Guowen Zhang Xiaojuan Xin Hui Hu Wei Qiu Dandan Ruan Yan Zhao |
author_sort |
Hui Xue |
title |
Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
title_short |
Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
title_full |
Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
title_fullStr |
Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
title_full_unstemmed |
Mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
title_sort |
mechanism of ultrasound and tea polyphenol assisted ultrasound modification of egg white protein gel |
publisher |
Elsevier |
publishDate |
2021 |
url |
https://doaj.org/article/665a638e539b4ed3b7b520b2c0681dbd |
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