• 한국응용과학기술학회지
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• 제24권4호
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• pp.362-368
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• 2007

To study the relationship between elementary biochemical states and structural states of the actomyosin crossbridges in muscle, the effects of binding of MgADP to myosin heads in the rigor muscle were examined by X-ray diffraction using synchrotron radiation. X-ray diffraction studies have been made to investigate the effects of binding of ADP on the structure of glycerinated rabbit skeletal muscle in the rigor state. The intensity increase was accompanied by a slight but distinct decrease in the 5.9 am layer-line intensity close to the meridian. These results strongly suggest that myosin heads altered their attached conformation in the proximal end toward the plane perpendicular to the fiber axis when MgADP was bound to them. We found that the intensity of the 14.5 nm-based meridional reflections increase by 20-50% when MgADP was added to the rigor muscle in the presence of hexokinase and myokinase inhibitor.

• Asian-Australasian Journal of Animal Sciences
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• 제20권7호
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• pp.1127-1134
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• 2007

Gels were made from surimi-like pork (SLP) made from muscles obtained at 1, 24 and 72 h post-mortem. The SLP from pre-rigor muscle had higher pH and moisture percentage compared to in- or post-rigor muscles. Also, SLP from pre-rigor muscle showed higher concentration of water-soluble protein that was washed out during the process. Gel from post-rigor muscle exhibited higher a* and b* value, and also resulted in higher Chroma and lower hue values. The dark color of gel from post-rigor muscle was related to higher concentration of sarcoplasmic protein in SLP and denser structure in the gel matrix. SDS-PAGE showed higher intensity of the phosphorylase in the sarcoplasmic protein fraction from pre-rigor muscle. Gel from post-rigor muscle showed higher hardness and sensory firmness, and the greater firmness was related to higher concentration of protein in SLP, and a compact network with smaller pockets in the gel matrix.

• Animal Bioscience
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• 제36권9호
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• pp.1445-1452
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• 2023

Objective: This study was performed to evaluate the quality characteristics of pork sausage (PS) with sea tangle extract (STE) and rapid chilled pre-rigor muscle (RCPM) for the development of reduced-salt low-fat sausage. Methods: Pre- and post-rigor pork ham muscles were prepared to process PSs. Positive control (reference, REF) using post-rigor muscle were manufactured at a regular-salt level of 1.5%. Fresh and rapid-chilled pre-rigor muscle (FPM and RCPM) were used to manufacture reduced-salt sausages with 0.8% salt. Reduced-salt PSs were prepared with four treatments: FT1 (FPM alone), FT2 (FPM with 5% STE), RT1 (RCPM alone), and RT2 (RCPM with 5% STE). The physicochemical and textural properties of the sausages with reduced-salt levels and RCPM combination were measured to determine if the characteristics of RCPM were similar to those with FPM. Results: The pH values of PS with FPM and RCPM were higher than those of REF with post-rigor muscle. Color values (L^*, a^*, b^*) were not affected by different rigor-states and salt addition level. Textural properties of reduced-salt PSs were similar to those of REF due to the improved functionalities of pre-rigor muscle. RT2 had lower expressible moisture (%) than other treatments with post-rigor muscle and RCPM except for RT1. Conclusion: The addition of STE and RCPM to reduced-salt PS increased the water-holding capacity, which was lower than those of PS with STE using RCPM but similar to those of regular-salt sausage.

• 한국생명과학회:학술대회논문집
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• 한국생명과학회 2005년도 국제학술심포지움 The 44th Annual Meeting of Korean Society for Life Science
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• pp.205-205
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• 2005

• Journal of Animal Science and Technology
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• 제64권3호
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• pp.397-408
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• 2022

Rinse & Chill^® technology (RCT) entails rinsing the vasculature using a chilled isotonic solution (3℃; 98.5% water and a blend of dextrose, maltose, and sodium phosphates) to rinse out the residual blood from the carcass. Infusion of pre-chilled solutions into intact animal carcasses immediately upon exsanguination is advantageous in terms of lowering the internal muscle temperature and accelerating chilling. This technology is primarily used for purposes of effective blood removal, favorable pH decline, and efficient carcass chilling, all of which improve meat quality and safety. Although RCT solution contains some substrates, the pre-rigor muscle is still physiologically active at the time of early postmortem and vascular rinsing. Consequently, these substrates are fully metabolized by the muscle, leaving no detectable residues in meat. The technology has been commercially approved and in continuous use since 2000 in the United States and since 1997 in Australia. As of January 2022, 23 plants have implemented RCT among the 5 countries (Australia, US, Canada, New Zealand, and Japan) that have evaluated and approved RCT. All plants are operating under sound Sanitation Standard Operation Procedures (SSOP) and a sound Hazard Analysis Critical Control Point (HACCP) program. No food safety issues have been reported associated with the use of this technology. RCT has been adapted by the meat industry to improve product safety and meat quality while improving economic performance. Therefore, this review summarizes highlights of how RCT technically works on a variety of animal types (beef, bison, pork, and lamb).