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Asian-Australas J Anim Sci > Accepted Articles
DOI: https://doi.org/10.5713/ajas.18.0780    [Accepted] Published online March 7, 2019.
The influence of ultrasound and adenosine 5’-monophosphate marination on tenderness and the structures of myofibrillar proteins of beef
Ye Zou1, Heng Yang2, Muhan Zhang1, Xinxiao Zhang1, Weimin Xu1, Daoying Wang1,*
1Institute of Agro-product Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China
2College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210046, China
Correspondence:  Daoying Wang, Tel: +86-25-84390065, Fax: +86-25-84390065, Email: daoyingwang@yahoo.com
Received: 16 October 2018   • Revised: 30 December 2018   • Accepted: 14 February 2019
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.


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.


The results showed that UAMP significantly increased MFI 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 α-helix and decrease in β-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.
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.
Keywords: Ultrasound; Adenosine 5’-Monophosphate; Tenderization; Myofibrillar Fragmentation Index; Synchronous Fluorescence Spectra
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