Effect of ice-temperature storage on some properties of salt-soluble proteins and gel from chicken breast muscles

Abstract

The changes in physicochemical properties of salt-soluble proteins and gel prepared with chicken breast muscles during −1.5oC (ice-temperature) and 4oC (refrigerated temperature) storage were investigated. Compared with the samples of 4oC stored group, the decrease in solubility, the content of total sulfhydryl and available sulfhydryl groups of SSP from chicken breast muscles at −1.5oC storage was effectively delayed, and the increase of both surface hydrophobicity and content of disulfide bond was obviously inhibited. The gel prepared with −1.5oC stored samples had much higher holding capacity of water, lower cooking loss, better springiness, and more uniform three-dimensional network structures with smaller-sized pores than those from 4°C stored-samples. Additionally, great changes in the proportions of non-flowing water and free water ratio were observed during 4oC storage. In short, the ice-temperature storage used for chicken meat preservation was better than refrigerated storage.

Keywords

• ice-temperature storage
• salt-soluble protein
• gel
• physico-chemical properties
• chicken breast muscles