|
| Effects of processing conditions on the solubility and structure of alcohol leached soybean protein concentrate |
| |
| DOI： |
| KeyWord:alcohol leached soybean protein concentrate solubility protein structure |
| FundProject:国家自然科学基金项目(U21A20270);国家重点研发计划项目(2017YFD0400200) |
| Author Name | Affiliation | | ZHAO Fangyuan1, GUO Xingfeng1, ZHAO Shuchao2,
ZHANG Ming3, YANG Ying1 | 1.School of Food Science and Technology, Henan University of Technology, Zhengzhou 450001, China；
2.Shandong Chemsta Machinery Manufacturing Co. , Ltd. , Jining 272000, Shandong, China；
3.Jining Machinery Design and Research lnstitute,Jining 272000, Shandong, China |
|
| Hits: 1440 |
| Download times: 1661 |
| Abstract: |
| To explore the reasons for the low solubility of alcohol leached soybean protein concentrate in industrial production, the effects of processing conditions(ethanol volume fraction, leaching temperature and drying temperature) on the solubility and structure of soybean protein concentrate were studied. The results showed that the solubility of soybean protein concentrate showed a trend of decreasing and then increasing with the increase of ethanol volume fraction, with the lowest solubility at an ethanol volume fraction of 65%. The solubility decreased significantly with the increase of extraction temperature and drying temperature. The surface hydrophobicity, the hydrophobic interaction between molecules, the content of disulfide bond and the particle size of soybean protein concentrate increased first and then decreased, and the maximum value was when the ethanol volume fraction was 65%; the α-helix content increased, β-sheet content first increased and then decreased, the random coil content decreased. With the increase of leaching temperature and drying temperature, the hydrogen bond interaction between molecules decreased, the surface hydrophobicity, the hydrophobic interaction between molecules, the content of disulfide bond and the particle size of soybean protein concentrate increased, the α-helix changed to β-sheet and random coil which indicated that the protein structure tended to disorder. In summary, the increase of protein surface hydrophobicity, the increase of intermolecular aggregation degree and other protein structure changes caused by the industrial alcohol processing process (60%-70% ethanol volume fraction, 50-60 ℃ leaching temperature, 60-70 ℃ drying temperature) lead to the decrease of protein solubility, which is not conducive to later application. |
| View full text View/Add Comment Download reader |
| Close |
|
|
|
