Effect of Pea Protein on Physicochemical Properties of Salt-soluble Protein of Pork

The salt-soluble protein was extracted from the longissimus dorsi muscle of pigs. And the effects of different contents pea protein(2%,4%,6%,8%,10%)on the physicochemical properties(solubility,surface hydrophobicity,sulfhydryl group,disulfide bond content,emulsifying property)of salt-soluble protein from pork were studied. Results indicated that the bands of myosin heavy chain,C-protein,α-actinin and myosin light chain in salt-soluble protein became narrower and lighter with the increasing of pea protein addition. Both the actin in salt-soluble protein and vicilin(7S)subunit in pea protein,the troponin T in salt-soluble protein and legA in pea protein were similar in molecular weight,and the bands became thicker and much colored. Compared with the control(without addition of pea protein),the surface hydrophobicity and emulsifying property of salt-soluble protein increased significantly(p<0.05)when the amount of pea protein was among 2% and 6%. The difference was not significant(p>0.05)when pea protein amount was in the range of 8% and 10%. With the increasing of pea protein addition,the content of turbidity and disulfide bonds increased,and content of disulfide bonds was up to 2.196 mol/10⁵ g when pea protein addition amount was up to 10%,and both the total sulfhydryl and free sulfhydryl content decreased. Additionally,the solubility increased firstly and then decreased,and it reached the maximum value of 42.88% when the added amount was 4%.It suggested that pea protein with proper amount could have a significant effect on the physicochemical properties of salt-soluble protein from pork.