The rise of thawing drip: Freezing rate effects on ice crystallization and myowater dynamics changes
文献类型: 外文期刊
作者: Qian S.; Hu F.; Mehmood W.; Li X.; Zhang C.; Blecker C.
作者机构:
关键词: Crystal structure; Ice; Mammals; Muscle; Reservoirs (water); Thawing; Dynamic changes; Free water; Freeze/thaw; Freezing rate; Ice crystallization; Longissimus dorsi; Myowater migration; Rate effects; Thaw loss; Ultra-fast; Freezing; ice; muscle protein; proton; water; animal tissue; Article; beef; bovine; controlled study; crystallization; density; freeze thawing; hydrophobicity; longissimus muscle; molecular dynamics; muscle fibril; nonhuman; particle size; protein secondary structure; solubility; surface property; animal; crystallization; freezing; muscle fibril; Animals; Cattle; Crystallization; Freezing; Ice; Myofibrils; Water
期刊名称: Food Chemistry
ISSN: 0308-8146
年卷期: 2022 年 373 卷
页码:
收录情况: SCIE(2022版) ; EI(2022版)
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. © 2021 Elsevier Ltd
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