| On the basis of the antihypertensive peptides prepared from pepper seed protein，the processing properties of antihypertensive peptides were studied. The enzymatic hydrolysate of pepper seed protein was purified through ultrafiltration membrane with relative molecular weight cutoff（MWCO）5 kDa，then the amino acid compositions of different relative molecular weights were determined. The physicochemical property of retentate and effect of in vitro gastrointestinal protease on inhibitory activity of angiotensin converting enzyme （ACE） were investigated. The results showed that the ACE inhibitory activity of permeate of pepper seed protein enzymatic hydrolysate improved after ultrafiltration，reaching 78.76%. The amino acid composition of antihypertensive peptides was complete，and the content of glutamic acid was the highest. The solubility of retentate was good in a wide range of pH(2.0-10.0),and its oil absorbency was high;with pH rising from 2.0 to 10.0,the foaming property of retentate first reduced then increased, while the foam stability was opposite;the emulsifying ability of retentate improved with the increase of pH,while the emulsion stability first decreased then went up;heat treatment (60-95℃),light,pH and sugar had small influence on ACE inhibitory activity of antihypertensive peptides. Meanwhile，when the antihypertensive peptides were digested by gastrointestinal protease，its ACE inhibitory activity changed a little，which were resistant to digestion. |
