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.

Changes in proteolytic enzyme activities, tenderness-related traits, and quality properties of spent hen meat affected by adenosine 5′-monophosphate during cold storage

“…The ionic strength of AMP leads to the alteration of the meat surface environment, thus affecting its stronger capacity to retain water ( Shao et al., 2016 ) and the creation of more space within myofibrils to avoid intracellular release of water ( Honikel et al., 1986 ). These significant findings corresponded to previous studies on the semimembranosus muscle of cattle ( Zou et al., 2019 ) and duck breast meat ( Wang et al., 2015 ).…”

Ultrasonic‐assisted phosphate curing: a novel approach to improve curing rate and chicken meat quality

“…1b]. This effect was similar to that of ultrasound-assisted sodium bicarbonate curing on tender chicken breast, which was reported by Xiong et al (2020 andZou et al (2019b). Gonzalez-Gonzalez reported that ultrasonic treatment tenderised and accelerated beef maturation (Gonzalez-Gonzalez et al, 2020).…”

“…(2020 and Zou et al . (2019b). Gonzalez‐Gonzalez reported that ultrasonic treatment tenderised and accelerated beef maturation (Gonzalez‐Gonzalez et al ., 2020).…”

“…Studies have demonstrated that ultrasound is a new approach to reduce the phosphate content in emulsified sausage (Pinton et al ., 2019) and frankfurter‐type sausages that enable phosphate reduction by 50% (Zhang et al ., 2021). Ultrasound technique combined with adenosine 5′‐monophosphate or brine (including sucrose, sodium tripolyphosphate, sodium pyrophosphate, and sodium hexametaphosphate) curing has been reported to have a synergistic effect that improves beef tenderness and WHC; this mechanism has been related to protein degradation and modification (Kang et al ., 2017; Zou et al ., 2019b). Additionally, studies have revealed that sodium bicarbonate (Xiong et al ., 2020), low‐concentration sodium bicarbonate (Zou et al ., 2019a), and sodium hypochlorite‐assisted (Sun et al ., 2019) curing are the effective methods for accelerating curing and tenderising tough meat.…”

Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties

“…Sriket et al [33] indicated that MHC was more likely to cause protein degradation than other proteins. Thus, it is most likely that the turbulent flow and shear force associated with ultrasonic cavitation dissociated the complex structure of MPs [2] , [34] and increased their accessibility. This makes MHC in MPs vulnerable to fragmenting into small particles, in effect leading to protein degradation in the present study.…”