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

Abstract

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 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. 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.

Keywords

• Ultrasound
• Adenosine 5′-Monophosphate
• Tenderization
• Myofibrillar Fragmentation Index
• Synchronous Fluorescence Spectra