[Objective] The mechanism of the nature change of peanut protein isolated in ultra-high pressure (UHP) processing was preliminarily researched. [Method] The peanut protein isolated being taken as raw material, the effect of UHP treatment on molecular structure was preliminarily researched by means of the method of SDS-PAGE, infrared spectroscopy, differential scanning calorimetry and scanning electron microscope. [Results] It was founded that the subunit of protein molecule was separated by means of the method of SDS-PAGE. It was founded that the protein degradation was strengthened with IR detection; there was high ionization extent in solution of the whole protein molecule and the distribution of the charge at molecular was increased. Through the differential scanning calorimetry cytometry, it was showed that under the lower the pressure( ≤400 MPa) , the peanut protein was degraded, becoming subunit, and then the subunit-extending gradually, which made the polar group and the internal hydrophobic group inside globular protein being exposed. Under the scanning electron microscopy, the peanut protein particles became smaller under pressure. [Conclusion] The changes of the structure mentioned-above might be the reason of high pressure.
Ultra-high pressurePeanut protein isolatedMolecular structure
国家科技期刊平台
NSTL
维普
万方数据
