共查询到18条相似文献，搜索用时 171 毫秒
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钙蛋白酶蛋白系统是影响肌肉生长和宰后肉嫩化的一个重要因素,主要由钙蛋白酶(μ-calpain和m-cal-pain)、钙蛋白酶抑制蛋白(calpastatin,CAST)及骨骼肌特异性钙蛋白酶(muscle specific calpain,P94)组成,钙蛋白酶抑制蛋白是一种内源性专一抑制钙蛋白酶(calpain)活性的蛋白,参与了调控肌原纤维蛋白的降解并在其中发挥了关键作用。本文概述了钙蛋白酶系统、钙蛋白酶抑制蛋白的结构、功能及其对提高肉嫩度的作用。 相似文献
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动物钙蛋白酶系统基因与肉质嫩度关联研究进展 总被引：1，自引：0，他引：1
钙蛋白酶系统由钙激活中性蛋白酶I(μ-calpain,calpain l,CAPN1)、钙激活中性蛋白酶Ⅱ(m-calpain,calpain 2,CAPN2)及其内源性抑制剂钙蛋白酶抑制蛋白(calpastatin,CAST)3个部分组成,钙蛋白酶的活性会影响畜禽肌肉增长和肉的嫩度.对钙蛋白酶系统的特性、作用机理及其对肉质的影响进行了综述,并对其应用前景进行讨论. 相似文献
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嫩度是影响猪肉品质的重要性状之一,肉品的嫩度取决于肌肉结构及其相关蛋白质的变化程度。影响肌肉嫩度的因素有很多,其中钙蛋白酶系统在肌肉嫩化过程中发挥着重要作用。钙蛋白酶抑制蛋白是钙蛋白酶系统的成员之一,同时也为钙蛋白酶抑制蛋白基因的表达产物,钙蛋白酶抑制蛋白基因为调控猪肉品质的候选基因之一。作者对影响肌肉嫩度的因素、钙蛋白酶系统的结构和生理功能,以及钙蛋白酶系统和钙蛋白酶抑制蛋白基因型对猪肉嫩度的影响进行综述。 相似文献
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钙蛋白酶系统研究进展 总被引：5，自引：0，他引：5
钙蛋白酶系统主要是由钙蛋白酶类和钙蛋白酶抑制蛋白组成。钙蛋白酶细胞内主要的蛋白水解酶,参与神经发育、肌纤维降解、信号传导等过程。因此,钙蛋白酶系统在肌肉生长、改善肉的嫩度及治疗某些疾病等方面起着重要的作用。本文主要就其成员、结构、功能等方面作一综述。 相似文献
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CAST基因研究进展 总被引：1，自引：0，他引：1
CAST(calpastatin)基因是钙蛋白酶水解系统成员之一。在一定浓度的钙离子作用下,钙蛋白酶系统主要作用于细胞骨架蛋白、蛋白激酶和磷酸酶,还参与细胞内的信号传递。CAST能促使蛋白质降解减少,导致肌肉增长,还可识别CAPN与钙结合引起的构象变化并与之特异性结合,从而保证钙蛋白酶对底物只进行特定部位的水解。因此,可以通过激活钙蛋白酶或降低钙蛋白酶抑制蛋白的活性来提高肌肉的嫩度,改善肉质。最近的研究表明,CAST基因多态性与家畜的眼肌厚度和眼肌面积存在关联,有望成为提高家畜肉用性能的候选基因。 相似文献
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钙蛋白酶系统在动物屠宰后肌肉蛋白质水解和肌肉嫩化过程中发挥重要的作用;脂肪酸结合蛋白参与脂肪酸的转运代谢,影响肌肉的嫩度、风味和多汁性,与背膘厚、大理石花纹、嫩度和系水力等肉用性状有较高关联度;生肌调节因子在肌肉分化过程中可控制启动成肌细胞的融合和肌纤维的形成;肌肉生成抑制素是控制肌肉生长的负调控因子,影响畜禽瘦肉率、改善肉质性状的重要营养基因。作者综述了钙蛋白酶系统家族、脂肪酸结合蛋白基因、生肌调节因子和肌肉生长抑制素等影响肉牛肉品质性状的基因,以期在肉牛育种选择中找到使产肉量和肉质得到同步提高的途径,进一步通过标记辅助选择来改善肉牛的肉质性状。 相似文献
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Involvement of μ/m‐calpain in the proteolysis and meat quality changes during postmortem storage of chicken breast muscle 
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下载免费PDF全文 Liang Zhao Tong Xing Jichao Huang Yan Qiao Yulian Chen Ming Huang 《Animal Science Journal》2018,89(2):423-431
The objective of this study was to investigate the role of calpain isotypes, especially poultry‐specific μ/m‐calpain in the proteolysis and meat quality changes of chicken breast muscle during postmortem storage. Calpain activity was detected by casein zymography, while the degradation of titin, desmin and Troponin‐T was analyzed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and western blot. Meat quality indicators such as water holding capacity and tenderness were also studied. The correlation analysis between calpain activity, proteolysis and the changes in meat quality indicators indicated that there were strong correlations for μ‐calpain during the first 12 h of storage, while such strong correlations for μ/m‐calpain were only found in samples stored from 12 h to 7 days. Our study suggested that μ‐calpain played a major role in meat quality changes while μ/m‐calpain could also be involved but played a limited role in the proteolysis and meat quality changes during 12 h to 7 days postmortem storage of chicken breast muscle. 相似文献
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Fábio L. Cruz Elisa B. de Carvalho Eduardo M. Ramos Luciano J. Pereira Márcio G. Zangeronimo 《Journal of animal physiology and animal nutrition》2021,105(3):442-451
The objective was to conduct a systematic review to evaluate the effects of dietary supplementation with beta-adrenergic agonists on calpains and calpastatin activity in bovine muscle and changes in meat tenderness. A survey was conducted in June 2019 on Science Direct, Web of Science, Scopus, PubMed and Capes Periodicals, using four keyword combinations: agonist and calpain and cattle; agonist and calpain and bovine; agonist and calpain and heifers; agonist and calpain and steers. Thirteen studies were selected, 54% concluded that supplementation with beta-adrenergic agonists increases calpastatin activity, 23% observed increase in their gene expression and 23% reported no effect on activity or expression of this enzyme. Nine studies evaluated the influence of beta-adrenergic agonists supplementation on meat texture and all found an increase in shear force values. There is strong evidence that beta-adrenergic agonists may increase calpastatin activity in the muscle, causing damage to meat tenderness. 相似文献
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μ-calpain是钙蛋白酶系统中广泛存在于动物细胞中的一种依赖Ca2+激活的蛋白水解酶。在宰后肉品的熟化阶段,μ-calpain对肌肉中因肌原纤维的部分降解引起的肉品嫩度提高起着重要的作用。作者对calpain系统的组成、μ-calpain的结构、作用特点、功能、活性测定及其编码基因内的遗传变异与肉品嫩度相关分子标记的研究进行综述。 相似文献
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《The Professional Animal Scientist》2002,18(2):107-111
Meat tenderness is a major factor affecting the consumers’ assessment of meat quality. Collagen is an abundant connective tissue protein and is a contributing factor to variation in meat tenderness and texture. It is found in three specific regions in muscle and in various forms and types. Collagen molecules are bound together through intermolecular crosslinks that help provide structure and strength. These crosslinks are initially reducible, but over time are replaced by mature, thermally stable, and less soluble crosslinks. These mature crosslinks, rather than the total amount of collagen, are the key factors in collagen-related toughness. The proportion of mature to reducible crosslinks increases with age, resulting in older animals that often have less tender meat than younger animals. Collagen crosslinks are also affected by growth rate, nutrition, and genetics. Collagen plays major roles in cooked meat as well. As collagen fibrils are heated during cooking, they shrink, resulting in a fluid loss and less tender meat. They also act to hold muscle fibers together after shrinkage. Post-mortem degradation of collagen and the use of collagenases appear to play a role in providing the desired tenderness and texture by altering the connective tissue structure. Collagen is very important in maintaining acceptable texture; however, high amounts of crosslinks can greatly decrease tenderness and consumer acceptability. 相似文献
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Changes in the muscle proteome after compensatory growth in pigs 总被引：1，自引：0，他引：1
Lametsch R Kristensen L Larsen MR Therkildsen M Oksbjerg N Ertbjerg P 《Journal of animal science》2006,84(4):918-924
Sixteen female pigs (Duroc x Landrace x Large White) were divided into 2 groups, which had either free access to the diet (control group) or were feed-restricted from d 28 to 80 and then had free access to the diet (compensatory growth group). The sensory analysis showed that the pigs exhibiting compensatory growth produced meat with increased tenderness compared with control pigs (P < 0.05). To gain further knowledge of the influence of compensatory growth on meat tenderness, the sarcoplasmic protein fraction of muscle tissue was studied at the time of slaughter and 48 h postmortem using proteome analysis. At slaughter, 7 different proteins were found to be affected by compensatory growth: HSC70, HSP27, enolase 3, glycerol-3-phosphate dehydrogenase, aldehyde dehydrogenase E2, aldehyde dehydrogenase E3, and biphosphoglycerate mutase. The HSC70 and HSP27 both belong to the heat shock family and are known to play a role during muscle development. Hence, they may be affected by compensatory growth and increased protein turnover. Forty-eight hours after slaughter, 8 different proteins were found to be affected by compensatory growth: myosin light chain (MLC) II, MLC III, sulfite oxidase, chloride intracellular channel 1, 14-3-3 protein gamma, elongin B, and phosphohistidine phosphatase 14. The changes observed on MLC II and MLC III could be a consequence of enzymatic cleavage in the neck region of the globular myosin head domain that causes the release of MLC II and MLC III from the actomyosin complex. It has previously been hypothesized that compensatory growth results in an increased postmortem proteolysis; thus it was presumed that the intensity of some protein fragments would be affected by compensatory growth. However, the peptides that were found to be affected at 48 h postmortem were all full-length proteins. The 14-3-3 protein gamma has been proposed to play a role in the contraction of muscle during rigor and may thereby have an effect on meat tenderness. This study reveals some very interesting changes in the muscle proteome affected by compensatory growth, which may be useful in understanding the relationship among compensatory growth, protein turnover, and meat tenderness. 相似文献
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P Ertbjerg P Henckel A Karlsson L M Larsen A J M?ller 《Journal of animal science》1999,77(9):2428-2436
The objective of the study was to improve the understanding of the relationship between the effect of epinephrine plus exercise and meat tenderness. The calpain, calpastatin, and cathepsin B + L activities and postmortem proteolysis in porcine longissimus muscle were studied. The muscle glycogen stores were depleted in five pigs by s.c. injection of epinephrine (.3 mg/kg) at 15 h antemortem and exercise on a treadmill (5 min, 3.8 km/h) immediately before slaughter. Antemortem injection of epinephrine and treadmill exercise resulted in higher ultimate pH (6.32 vs 5.66 in control) and decreased (P < .05) thaw loss, cooking loss, and shear force values. The muscle energy depletion treatment increased (P < .05) the muscle mu-calpain activity measured 42 min postmortem, and at 24 h mu-calpain activity was still approximately 50% greater in the high ultimate pH group. Also, as the ratio of mu-calpain to calpastatin increased (P < .01), the overall proteolytic potential of the calpain system were greater. These observations suggest that the muscle energy level may influence the activity of the calpain system in the living animal. The high ultimate pH group showed lower (P < .001) cathepsin B + L activity in the myofibrillar and the soluble fractions after 8 d of storage, suggesting that the increased ultimate pH increased the stability of the lysosomal membrane and thereby reduced the release of cathepsins from the lysosomes during storage. The SDS-PAGE showed increased (P < .001) degradation of a 39-kDa band in the epinephrine and exercise-treated samples. Degradation products at 30, 31, and 32 kDa were labeled by troponin-T antibody in western blot. An appearing 24-kDa band was identified as a troponin-I degradation product in western blot. The proteolytic degradation pattern of myofibrillar proteins during storage differed in control and treated samples, supporting the hypothesis that calpain-mediated proteolysis was affected after treatment, resulting in meat with high ultimate pH. 相似文献