The influence of ultrasound and adenosine 5 '-monophosphate marination on tenderness and structure of myofibrillar proteins of beef

文献类型： 外文期刊

第一作者： Zou, Ye

作者： Zou, Ye;Zhang, Muhan;Zhang, Xinxiao;Xu, Weimin;Wang, Daoying;Yang, Heng

作者机构：

关键词： Ultrasound; Adenosine 5 '-Monophosphate; Tenderization; Myofibrillar Fragmentation Index; Synchronous Fluorescence Spectra

期刊名称：ASIAN-AUSTRALASIAN JOURNAL OF ANIMAL SCIENCES （ 影响因子：2.509； 五年影响因子：2.604 ）

ISSN： 1011-2367

年卷期： 2019 年 32 卷 10 期

页码：

收录情况： SCI

摘要： Objective: The aim was to investigate the influence of ultrasound and adenosine 5'-monophosphate (AMP) marination (UAMP) on tenderness and structure of myofibrillar proteins of beef. Methods: Five groups, the untreated meat (Control), deionized water marination (DW), ultrasound followed by DW (UDW), AMP marination (AMP), and ultrasound followed by AMP (UAMP) were studied. Myofibrillar fragmentation, cooking loss, shear force, thermograms, histological observation of meats and myofibrillar proteins properties were investigated in these different treatments. Results: The results showed that UAMP significantly increased myofibrillar fragmentation index from 152 (Control), 231 (AMP), and 307 (UDW) to 355 (p< 0.05), respectively. The lowest cooking loss, shear force and peak denaturation temperature were observed in UAMP. In histological observation, UDW and UAMP had more fragmented muscular bundles than the others. Furthermore, a drastic increase in a-helix and decrease in beta-sheet of myofibrillar proteins was observed in UAMP, implying the disaggregation of protein samples. The synchronous fluorescence spectra of myofibrillar proteins in UAMP suggested the combination of ultrasound and AMP could accelerate the unfolding molecular structure and destroying hydrophobic interactions. The results of circular dichroism and synchronous fluorescence spectra for myofibrillar proteins coincided with the microstructures of beef. Conclusion: The results indicate that ultrasound combined with AMP improved meat tenderness not only by disruption in muscle integrity, increasing water retention, but also altering their spatial structure of myofibrillar proteins.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序