肌原纤维
海藻糖
化学
溶解度
变性(裂变材料)
食品科学
生物化学
色谱法
核化学
有机化学
作者
Shengjun Wu,Shaowei Pan,Hongbin Wang
标识
DOI:10.1016/j.foodchem.2014.03.100
摘要
The effect of trehalose on the denaturation of weever (Lateolabrax japonicus) myofibrillar protein during frozen storage at −18 °C for 90 d was investigated. Trehalose (2.5–10 g dry weight) was added to 100 g of myofibrillar protein, and changes in the Ca2+-adenylpyrophosphatase (ATPase) activity, solubility, sulfhydryl content, and unfrozen water content of myofibrils were examined during frozen storage. Ca2+-ATPase activity and myofibrillar protein solubility decreased gradually during frozen storage at −18 °C upon addition of trehalose. By contrast, Ca2+-ATPase activity and myofibrillar protein solubility in the control group dropped drastically during the first 45 d of storage and then further decreased gradually for up to 90 d of storage, indicating a biphasic denaturation pattern. Trehalose addition significantly increased sulfhydryl and unfrozen water contents in the myofibrillar protein of the treatment groups compared with that of the control group (p < 0.05) during frozen storage at −18 °C.
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