コイ筋形質タンパク質画分の加熱処理による物理化学的性状と乳化活性の変化

概要

論文の詳細を見る
Sarcoplasmic protein (Sp-P) from carp Cyprinus carpio was heated at various temperatures from 20 to 100°C for 15 min at pH 7.0, and the physicochemical properties and emulsifying activity of heat-treated Sp-P were investigated. By treatment above 40°C, the solubility of Sp-P decreased and its surface hydrophobicity and reactive SH content increased with a rise in heating temperature. For the soluble fraction of heat-treated Sp-P, the surface hydrophobicity and total SH contents at 50-100°C treatment were somewhat smaller than those at 20-40°C. A 12 kDa component largely remained soluble at 70°C or above and was assumed to be parvalbumin. The emulsifying activity of Sp-P was minimal at 60°C, and thus it was considered to be attributable to heat-coagulable soluble proteins for the lower temperature treatment and to parvalbumin for the higher temperature treatment.
日本水産學會の論文