肌原纤维
化学
微观结构
碎片(计算)
背最长肌
生物物理学
生物化学
分析化学(期刊)
色谱法
食品科学
结晶学
生物
生态学
作者
Guangyu Wu,Chuan Yang,Heather L. Bruce,Bimol C. Roy,Xia Li,Chunhui Zhang
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2022-12-22
卷期号:409: 135266-135266
被引量:22
标识
DOI:10.1016/j.foodchem.2022.135266
摘要
The current study investigates the influence of alternating electric field (AEF)-assisted freezing-thawing-aging sequence on the muscle microstructure and myofibrillar protein characteristics. Three treatments were used for longissimus dorsi (LD) muscle: only aging (OA), freezing-thawing-aging sequence (FA) and AEF-assisted freezing-thawing-aging sequence (EA). Compared with the FA and EA groups, the OA group showed considerably fewer cracks between muscle fibers and maintained the integrity of the Z-line as observed using scanning and transmission electron microscopy, respectively. Furthermore, the EA treatment effectively decreased myofibrillar fragmentation, myofibrillar protein aggregation, and protein oxidation, as shown by the myofibrillar fragmentation index, turbidity, and total sulfhydryl concentration. Analysis of surface hydrophobicity and the Fourier transform infrared, UV absorption, and fluorescence spectrums indicated that AEF minimized the alterations of protein secondary and tertiary structure alterations during aging after freezing.
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