Isoelectric solubilization/precipitation processing modified sarcoplasmic protein from pale, soft, exudative-like chicken meat

Abstract

The sarcoplasmic protein from pale, soft and exudative -like chicken breast meat was modified using an isoelectric solubilization/precipitation process. After the modification, the sarcoplasmic protein obtained a larger particle distribution than the nontreated sample, indicating a severe aggregation. The isoelectric solubilization/precipitation-treated sarcoplasmic protein aggregates exhibited a flocculated and amorphous shape stabilized by the hydrophobic interactions. The hydrophobic interactions of alkali-treated sarcoplasmic proteins were relatively constant during heating, while they dramatically increased in nontreated sample. The alkali-treated sarcoplasmic protein could promote myofibrillar protein gelation properties, as proved by the higher breaking force and lower cooking loss. According to our results, it is hypothesized that the alkali-treated sarcoplasmic protein likely does not interfere in the gelation behavior of myofibrillar protein but does fill in the pores of the three-dimensional network, thereby strengthening its gelation elasticity. Overall, the alkali-treated sarcoplasmic protein exhibits the potential to improve the myofibrillar protein gelation properties.