Foaming, emulsifying properties and surface hydrophobicity of soy proteins isolate as affected by peracetic acid oxidation. Issue 1 (1st January 2019)
- Record Type:
- Journal Article
- Title:
- Foaming, emulsifying properties and surface hydrophobicity of soy proteins isolate as affected by peracetic acid oxidation. Issue 1 (1st January 2019)
- Main Title:
- Foaming, emulsifying properties and surface hydrophobicity of soy proteins isolate as affected by peracetic acid oxidation
- Authors:
- Li, Junsheng
Wang, Bixuan
Fan, Junfu
Zhong, Xin
Huang, Guoxia
Yan, Liujuan
Ren, Xiane - Abstract:
- ABSTRACT: In this study, the effects of the disulfide bond cleavage induced by peracetic acid oxidation on the surface properties and surface hydrophobicity of soy proteins isolate (SPI) were investigated. The surface hydrophobicity, foaming capacity and emulsifying capacity of oxidized-SPI increased gradually at the initial stage with the increase of peracetic acid concentration. When the concentration of peracetic acid was increased up to 0.4%, compared with that of native SPI, the surface hydrophobicity, foaming capacity, emulsifying capacity and emulsifying stability of oxidized-SPI increased by 114.0, 81.4, 65.2, 49.8%, respectively, and achieved optimal results. However, excessive oxidation led to a decrease in surface hydrophobicity, foaming capacity and emulsifying stability of SPI, but it had no obvious effect on the foaming stability and emulsifying capacity of SPI. The foaming capacity, emulsifying capacity and emulsifying stability of SPI were positively related to the changes of surface hydrophobicity which caused by disulfide bond cleavage. The results of fluorescence spectroscopy, CD spectroscopy, and particle size analysis showed that the disulfide bond cleavage did cause great changes in the molecular structure of SPI, but there was no clear correlation between the molecular structural change and the surface activity of SPI. These suggested that the improvement of foaming capacity, emulsifying capacity and emulsifying stability of SPI could be achieved byABSTRACT: In this study, the effects of the disulfide bond cleavage induced by peracetic acid oxidation on the surface properties and surface hydrophobicity of soy proteins isolate (SPI) were investigated. The surface hydrophobicity, foaming capacity and emulsifying capacity of oxidized-SPI increased gradually at the initial stage with the increase of peracetic acid concentration. When the concentration of peracetic acid was increased up to 0.4%, compared with that of native SPI, the surface hydrophobicity, foaming capacity, emulsifying capacity and emulsifying stability of oxidized-SPI increased by 114.0, 81.4, 65.2, 49.8%, respectively, and achieved optimal results. However, excessive oxidation led to a decrease in surface hydrophobicity, foaming capacity and emulsifying stability of SPI, but it had no obvious effect on the foaming stability and emulsifying capacity of SPI. The foaming capacity, emulsifying capacity and emulsifying stability of SPI were positively related to the changes of surface hydrophobicity which caused by disulfide bond cleavage. The results of fluorescence spectroscopy, CD spectroscopy, and particle size analysis showed that the disulfide bond cleavage did cause great changes in the molecular structure of SPI, but there was no clear correlation between the molecular structural change and the surface activity of SPI. These suggested that the improvement of foaming capacity, emulsifying capacity and emulsifying stability of SPI could be achieved by changing its surface hydrophobicity via peracetic acid oxidation. … (more)
- Is Part Of:
- International journal of food properties. Volume 22:Issue 1(2019)
- Journal:
- International journal of food properties
- Issue:
- Volume 22:Issue 1(2019)
- Issue Display:
- Volume 22, Issue 1 (2019)
- Year:
- 2019
- Volume:
- 22
- Issue:
- 1
- Issue Sort Value:
- 2019-0022-0001-0000
- Page Start:
- 689
- Page End:
- 703
- Publication Date:
- 2019-01-01
- Subjects:
- Soy proteins isolate -- peracetic acid oxidation -- disulfide bond cleavage -- surface properties -- surface hydrophobicity
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664.0705 - Journal URLs:
- http://www.tandfonline.com/toc/ljfp20/current ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/10942912.2019.1602540 ↗
- Languages:
- English
- ISSNs:
- 1094-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4542.253100
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16971.xml