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快速生长型和慢速生长型鸡肉胸肉和腿肉中天然肌球蛋白和肌动蛋白的理化特性:比较研究。

Physico-chemical properties of natural actomyosin from breast and thigh meat of fast- and slow-growing chicken: a comparative study.

机构信息

School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.

School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.

出版信息

Poult Sci. 2024 Nov;103(11):104153. doi: 10.1016/j.psj.2024.104153. Epub 2024 Aug 2.

Abstract

Physico-chemical behaviors of natural actomyosin (NAM) from slow-growing Korat chicken (KC) breast and thigh at low (0.2 M) and high (0.6 M) NaCl concentrations were evaluated and compared to those from their corresponding muscles in fast-growing broiler chicken (BC). NAM from KC breast and thigh meat showed higher solubility than their corresponding in BC (p < 0.05). Breast NAM from both chickens showed the highest solubility at 0.4 M NaCl, while thigh NAMs showed the highest solubility at 0.8 M (p < 0.05). SDS-PAGE revealed higher protein extractability for breast NAMs at low ionic strength, regardless of breed and structural protein, particularly troponin, appeared to vary within muscle and breed. NAM from KC showed higher Ca-ATPase activity, surface hydrophobicity, but lower total sulfhydryl groups content (p < 0.05). Particle size of NAM solutions varied with ionic strength, in which KC-NAM showed larger size than at lower ionic strength, while BC-NAM appeared to be greater at higher ionic strength. NAM from KC breast showed higher thermal stability as higher initial (T) and maximum (T) denaturation temperatures of 48.4 and 54.8°C, respectively, recorded by microdifferential scanning calorimetry. The KC-NAM, particularly from breast, exhibited lower turbidity within 40-50°C, while turbidity increased in BC samples at low ionic strength when heated at 60°C. Dynamic rheology revealed different storage modulus (G') depending on breed, muscle type and ionic strength. Breast BC-NAM formed more elastic gel with higher end point G' at 80°C (G; p < 0.05). Ionic strength showed reverse effects on different breeds as a stronger G value achieved in KC- NAM at low ionic strength, while high ionic strength induced stronger gel in BC samples. Aggregation of NAMs began at lower temperatures at higher ionic strength and actin dissociation probably occurred in breast NAM from KC as observed by a drop of G' at around 70°C. The results of this study revealed differences between NAM of the two breeds, by which higher gel elasticity are expected in KC at lower ionic strength.

摘要

从慢速生长的科拉特鸡(KC)鸡胸和大腿中提取的天然肌球蛋白(NAM)在低盐(0.2 M)和高盐(0.6 M)浓度下的物理化学行为,并与快速生长的肉鸡(BC)的相应肌肉进行了比较。KC 鸡胸和大腿肉中的 NAM 的溶解度高于 BC(p < 0.05)。两种鸡的胸 NAM 在 0.4 M NaCl 下表现出最高的溶解度,而腿 NAM 在 0.8 M 时表现出最高的溶解度(p < 0.05)。SDS-PAGE 显示,在低盐离子强度下,无论品种和结构蛋白如何,胸 NAM 的蛋白质提取率都更高,特别是肌钙蛋白似乎在肌肉和品种内有所不同。KC-NAM 的 Ca-ATPase 活性、表面疏水性较高,但总巯基含量较低(p < 0.05)。NAM 溶液的粒径随离子强度而变化,其中 KC-NAM 在较高离子强度下的粒径较大,而 BC-NAM 在较高离子强度下的粒径较大。KC 鸡胸 NAM 的初始(T)和最大(T)变性温度分别为 48.4°C 和 54.8°C,表明其热稳定性较高。通过微差示扫描量热法记录。KC-NAM,特别是来自胸肉的 NAM,在 40-50°C 范围内表现出较低的浊度,而在低离子强度下加热至 60°C 时,BC 样品的浊度增加。动态流变学显示,不同品种、肌肉类型和离子强度下的储存模量(G')不同。胸 BC-NAM 在 80°C 时形成更具弹性的凝胶,端点 G'更高(G;p < 0.05)。离子强度对不同品种有相反的影响,因为在低盐 KC-NAM 中达到更高的 G 值,而在高离子强度下,BC 样品形成更强的凝胶。在较高的离子强度下,NAM 的聚集在较低的温度下开始,并且在 KC 胸 NAM 中可能发生了肌动蛋白的解离,因为在大约 70°C 时 G'的下降表明了这一点。本研究结果揭示了两种品种 NAM 之间的差异,预计在低盐离子强度下 KC 的凝胶弹性更高。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2336/11471090/40a986496041/gr1.jpg

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