关键词: 巯基, 疏水性, 肌肉蛋白质, 乳化, 凝胶

Abstract:

The effect of changes in sulfhydryl content and surface hydrophobicity induced by chemical modification with
β-mercaptoethanol and Tween-80, respectively, on the emulsifying and gel properties of salt-soluble proteins of pork muscle
were examined and the roles of disulfide bonds and hydrophobic interactions in forming emulsions and gels were elaborated.
Free sulfhydryl content of salt-soluble protein solutions was increased with the addition of β-mercaptoethanol as a sulfhydryl
blocking agent and delayed gel formation and reduced overall viscoelasticity were observed, suggesting that blocking
the formation of disulfide bonds can deteriorate the heat-induced gelation characteristics of pork proteins. However, no
significant correlation between the free —SH content and emulsifying properties of pork proteins was observed. On the other
hand, higher surface hydrophobicity resulted in formation of less stable emulsions without significantly affecting the gel
properties. These data suggest that an appropriate degree of hydrophobicity may be of great significance for the formation of
stable emulsions and that disulfide bonds presumably contributes to good gel properties.

Key words: sulfhydryl, hydrophobicity, pork proteins, emulsion, gel