• Asian-Australasian Journal of Animal Sciences
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• 제26권3호
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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.

• 한국축산식품학회지
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• 제44권2호
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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.

• 한국축산식품학회지
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• 제35권4호
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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.

• 한국축산식품학회지
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• 제38권1호
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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.

• 한국식품과학회지
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• 제28권3호
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• pp.566-572
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• 1996

본 연구에서는 숙성 중 야기되는 식육의 인화정도를 파악할 수 있는 척도로서 이용하기 위하여, 근원섬유 Z선의 구성단백질의 하나인 zeugmatin에 대한 항체를 조제, 간접연역형광법으로 zeugmatin의 숙성중 변화와 근원섬유의 소편화와의 관계를 알아 보았다. Zeugmatin은 변성하기 쉬운 단백질로서 재래식 방법으로는 정제가 블가능하므로 이 단백질을 함유하는 획분을 정제과정 중에 채취하여 전기영동으로 전개, 이에 해당하는 band를 분리하여 polyclonal항체를 용이하게 받을 수 있었으며, 이 조제된 항체는 zeugmatin과 특이적으로 반응하였다. 조제된 항체를 이용하여 간접면역형광법으로 식육의 숙성중에 zeugmatin의 변화와 근원섬유의 소편화로 나타나는 식육의 연화와의 상관관계를 알아 본 결과, 이 두가지 변화는 특이적으로 일치하였다 즉, 닭의 흉근을 $4^{\circ}C$에서 숙성하면서 측정한 근원섬유의 소편화도는 도살 후 6시간에서 24시간 사이에 급속히 증가하여 이 시간대에 식육이 급속히 부드러워짐을 나타내었고, zeugmatin에 대한 항체가 나타내는 형광광도도 도살 후 6시간에서 24시간 사이의 동일한 시간대에 급적히 약화되어 zeugmatin이 이 시간대에 급속히 인화하였음을 나타내었다. 이상의 결과로 근원섬유 Z선의 구성단백질 중 하나인 zeugmatin은 숙성에 따라 야기되는 식육의 연화정도, 즉 식육의 숙성도를 나타내는 척도로서 이용될수 있으며, 그 이용방법으로는 간접면역형광법이 가장 간편한 방법인 것으로 판단되었다.

• Asian-Australasian Journal of Animal Sciences
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• 제22권2호
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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.

• 한국산업융합학회 논문집
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• 제22권5호
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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).

• 한국축산식품학회지
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• 제18권4호
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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.

• 한국축산식품학회:학술대회논문집
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• 한국축산식품학회 1996년도 추계심포지움 및 학술발표회
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• pp.12-19
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• 1996

• 한국식품영양학회지
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• 제11권5호
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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.