|
| Molecular structure and antigenicity analysis of enzymatic hydrolysates from soybean 7S globulin by heating and protease treatment |
| |
| DOI： |
| KeyWord:soybean 7S globulin heating enzymatic hydrolysis antigenicity β-conglycinin α subunit |
| FundProject: |
|
| Hits: 1429 |
| Download times: 608 |
| Abstract: |
| Soybean 7S globulin was hydrolyzed with different proteases under different heating pretreatment conditions. SDS-PAGE was used to investigate the degradation of soybean 7S globulin after enzymatic hydrolysis. Indirect competitive ELISA was used to detect the antigenicity of the hydrolysates.The results showed that the heating pretreatment combined with enzymatic hydrolysis could significantly increase the degradation of β-conglycinin. The digestibility of the β subunit was greatly improved and the α subunit and the α′subunit were almost completely degraded. The enzymatic hydrolysis rate of trypsin was faster than that of pepsin at the same enzymatic hydrolysis time. Heating pretreatment combined with enzymatic hydrolysis could significantly reduce the antigenicity of β-conglycinin and the effect of trypsin was better than that of pepsin. Meanwhile, heating at 80 ℃ for 10 min followed by trypsin hydrolysis treatment could decrease the antigenicity of soybean 7S globulin by 79.99%, while pepsin only could decrease by 50.4% under the optimal condition. SDS-PAGE results showed that the antidigestible fragments derived from the hydrolysates by pepsin and trypsin were derived from the α subunit of β-conglycinin, which was identified by mass spectrometry. |
| View full text View/Add Comment Download reader |
| Close |
|
|
|
