关键词: 明胶, 肌原纤维蛋白, 凝胶, 硬度, 贮能模量

Abstract:

The values of gel hardness and storage modulus G ＇ of compound gelatin-myofibrillar protein gels formed in the attendance of different reagents were measured in order to understand the forces involved in the gel formation. It was found that adding urea distinctly decreased gel hardness. This suggests that hydrogen bond is the most important force responsible for gel formation and maintenance at low temperatures. Gel hardness could be changed by adjusting pH or by separately adding DTT, potassium bromate or SDS, indicating all electrostatic force, disulfide bond and hydrophobic interaction make a contribution to gel formation and maintenance. Increasing pH during heating treatment resulted in a lower G＇ value. Additions of DTT, SDS and urea were all able to decrease G＇value, and the most obvious decrease was observed when SDS was added. Therefore, it can be concluded that hydrophobic interaction plays the most vital role in the heat-induced gel formation between gelatin and myofibrillar.

Key words: gelatin, myofibrillar protein, gel, hardness, storage modulus