化学
结晶
自由水
肌原纤维
冰晶
结晶水
凝结
热力学
地质学
气象学
生物化学
物理
有机化学
岩土工程
作者
Shuyi Qian,Feifei Hu,Waris Mehmood,Xia Li,Chunhui Zhang,Christophe Blecker
出处
期刊:Food Chemistry
[Elsevier]
日期:2022-03-01
卷期号:373: 131461-131461
被引量:42
标识
DOI:10.1016/j.foodchem.2021.131461
摘要
To better reveal the formation of thawing drip, this study investigated the ice crystallization and myowater dynamics changes in frozen bovine Longissimus dorsi muscle. In ultra-fast freezing a narrow distribution of ice crystals size was observed together with higher solubility, lower surface hydrophobicity and stable second structure of myofibrillar protein. Accordingly, ultra-fast freezing samples exhibited significantly lower thaw loss (4.35 %) than slow freezing (8.22 %) after 48 h of freezing. Upon thawing, 2D T1-T2 relaxation spectra indicated a myowater redistribution, in which slow freezing led to major migration of water from immobile water to free water. Besides, T1 and T2 relaxation times showed an increasing trend with freezing process. The proton density images displayed major free water seep from myofibrils to the surface of muscle. Consequently, the water from the "reservoir" (free water) flowed into the "channel" (the widened spaces between muscle fibres), and formed into the thawing drip.
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