• Asian-Australasian Journal of Animal Sciences
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• v.26 no.3
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• pp.443-454
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• 2013

Tenderness is the most important meat quality trait, which is determined by intracellular environment and extracellular matrix. Particularly, specific protein degradation and protein modification can disrupt the architecture and integrity of muscle cells so that improves the meat tenderness. Endogenous proteolytic systems are responsible for modifying proteinases as well as the meat tenderization. Abundant evidence has testified that calpains (CAPNs) including calpain I (CAPN1) and calpastatin (CAST) have the closest relationship with tenderness in livestock. They are involved in a wide range of physiological processes including muscle growth and differentiation, pathological conditions and post-mortem meat aging. Whereas, Calpain3 (CAPN3) has been established as an important activating enzyme specifically expressed in livestock's skeletal muscle, but its role in domestic animals meat tenderization remains controversial. In this review, we summarize the role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and analyse the relationship between CAPN3 and tenderness in domestic animals. Besides, the possible mechanism affecting post-mortem meat aging and improving meat tenderization, and current possible causes responsible for divergence (whether CAPN3 contributes to animal meat tenderization or not) are inferred. Only the possible mechanism of CAPN3 in meat tenderization has been confirmed, while its exact role still needs to be studied further.

• Food Science of Animal Resources
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• v.44 no.2
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• pp.239-254
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• 2024

This review sought to categorize studies on meat tenderization and safety through pulsed electric field (PEF) treatment, with a particular focus on reconciling conflicting findings regarding the tenderization effect (i.e., the primary outcome of PEF treatment) and to discuss the underlying mechanisms of these effects. While the tenderization effect may vary depending on the homogeneity of PEF treatment and variations in the conditions of texture measurements, the protein associated with tenderization was degraded by PEF treatment in most studies. PEF technology enables the delivery of a high voltage for a brief duration, typically in the microsecond range, making it a non-thermal technology. One of the distinct advantages of PEF is its ability to preserve the freshness of meat due to its exceptionally short treatment time. While PEF studies have traditionally centered on pasteurizing liquid foods, research on its application to meat is steadily expanding. Therefore, this review aims to elucidate the mechanisms of PEF and provide current insights into the applications of this technology for meat tenderization and microbial inactivation.

• Food Science of Animal Resources
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• v.35 no.4
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• pp.533-540
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• 2015

The aim of this study was to investigate the effects of aqueous extract from Sarcodon aspratus on tenderization of the bovine longissimus dorsi muscles in comparison with commercial proteolytic enzymes. Furthermore, meat quality and muscle protein degradation were examined. We marinated meat with 2% Sarcodon aspratus extract, 2% kiwi extract, and 0.2% papain. Beef chunks (3×3×3 cm³) were marinated with distilled water (control), Sarcodon aspratus extract (T1), kiwi extract (T2) or papain (T3) for 48 h at 4℃. There were no significant differences in muscle pH and lightness between control and treated samples. T1 had the lowest redness (p<0.01), and higher cooking loss and water holding capacity than control and T2 (p<0.05). T1 and T3 exhibited lower shear force values than control (p<0.05). Total protein solubility did not differ significantly between T1 and control, but T1 had less myofibrillar protein solubility than control and T2 (p<0.001). The degradation of myosin heavy chain in T1 and T3 was observed. This degradation of myofibrillar protein suggests that Sarcodon aspratus extract could influence tenderization. These results show that aqueous extract of Sarcodon aspratus extract actively affect the tenderness of the bovine longissimus dorsi muscle.

• Food Science of Animal Resources
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• v.38 no.1
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• pp.143-151
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• 2018

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak ($T_p$) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for post-mortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

• Korean Journal of Food Science and Technology
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• v.28 no.3
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• pp.566-572
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• 1996

The relationship between the myofibrillar fragmentation and zeugmatin during post-mortem aging was in vestigated by indirect immunofluorescence method using antizeugmatin Antiserum as a measure of meat tenderization. The antizeugmatin antiserum was prepared using bands separated by SDS-PAGE and reacted specifically with zeugmatin, showing no cross-reactivity with the other myofibrillar proteins. By the indirect immunofluorescence method, this antiserum stained the fresh myofibrillar However, the fluorescence intensity decreased with post-mortem time and almost disappeared within 24 hr of storage, in parallel with the myofibrillar fragmentation. It was therefore concluded that zeugmatin can be conveniently used as a measure of meat tenderization during post-mortem aging by immunoflurescence method.

• Asian-Australasian Journal of Animal Sciences
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• v.22 no.2
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• pp.282-288
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• 2009

The present paper describes the effects of pressure and post-mortem aging treatments on in situ proteasome activity in rabbit and bovine skeletal muscles. Synthetic peptide hydrolyzing activity of rabbit proteasomes remained in the muscle after exposure to pressures up to 100 MPa. However, when a pressure of 400 MPa or more was applied, proteasomes were markedly inactivated. The extraction of proteasomes from excessively pressurized muscle appeared to be difficult. Proteasomes in aged muscle remained relatively stable throughout the aging process, with activity after 168 h (7 days) being 35%, 48%, 53% and 31% of the 0 h post-mortem LLVY, LSTR, AAF and LLE total hydrolyzing activities, respectively. The synthetic peptide hydrolyzing activities of bovine muscle proteasomes were similar to those of rabbit skeletal muscle proteasomes. The results suggest that synthetic peptide hydrolyzing activity remains in muscle exposed to relatively low pressures. Furthermore, it is known that high-pressure treatment induces fragmentation of myofibrils, modification of actin-myosin interaction and activation of intramuscular proteinases, cathepsins and calpains. Thus, proteasomes are probably involved in the tenderization process in combination with other intramuscular proteinases under high-pressure conditions. Our findings confirmed that proteasomes play a role in meat tenderization induced by high-pressure treatment or aging.

• Journal of the Korean Society of Industry Convergence
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• v.22 no.5
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• pp.545-551
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• 2019

The purpose of this study was to investigate the effects of protease in kiwi fruit powder after freeze drying which has the ratio of 0%, 1%, 2%, and 3% on the tenderization of the bovine longissimus dorsi muscle. Beef loin chunks were marinated in distilled water (Control), 1% kiwi powder (K1), 2% kiwi powder (K2), and 3% kiwi powder (K3). As a result, the enzyme activities have shown to have higher activity (p<0.001) as the amount of freeze-dried kiwi powder increased. There are significant difference in pH (p<0.01), color of the beef were slightly different between the C (control) group and the sample groups. The cooking loss showed the highest value of K3 (p<0.001), and water holding capacity showed the highest value of K3. Furthermore, the sample groups exhibited lower shear force values compared with the control (p<0.001).

• Food Science of Animal Resources
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• v.18 no.4
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• pp.292-300
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• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 1996.11a
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• pp.12-19
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• 1996

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.580-584
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• 1998

Tenderization of beef by the addition of barks(Morus alba Linne) and its sensory properties were observed by shearing test, cooking loss, pH, protein content and sensory evaluation. Shear force was decreased as the addition level of barks (Morus alba Linne) increased. Tenderization effect of beef was increased 8,8% at the addition level of 2.5%, 25% at 5.0%, 4.7% at 7.5%, 58% at 10% barks(Morus alba Linne). Cooking loss was observed 44.50% at the no addition, 45.3% at 2.5%, 45.8% at 5.0%, 47.5% at 7.5%, 50.0% at 10% addition level of barks (Morus alba Linne). As the addition level of barks(Morus alba Linne) increased pH of cooked beef decreased to the range of 5.6 to 5.46. As the addition level of barks (Morus alba Linne) increaed protein content of beef decreased whereas protein content of cooled liquor increased. The addition of barks(Morus alba Linne) improved the sensory quality of cooked beef. Especially, tenderness scored the highest value in 10% added beef and other quality factors color, flavor, juiciness and overall quality were evaluated significantly high in 5% added beef. Therefore 5% addition level of barks(Morus alba Linne) for cooking beef was suggested as the desirable level of addition.