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肉的结合质量与肌原纤维蛋白之间的关系:IV. 肌球蛋白B中天然原肌球蛋白和肌动蛋白对热凝固碎肉凝胶流变学特性的贡献。

RELATIONSHIPS BETWEEN BINDING QUALITY OF MEAT AND MYOFIBRILLAR PROTEINS: IV. Contribution of Native Tropomyosin and Actin in Myosin B to Rheological Properties of Heat Set Minced-Meat Gel.

作者信息

Nakayama Teruo, Sato Yasushi

机构信息

Laboratory of Food Science and Technology (Animal Products), Faculty of Agriculture, Nagoya University, Nagoya, Japan.

出版信息

J Texture Stud. 1971 Dec;2(4):475-488. doi: 10.1111/j.1745-4603.1971.tb00595.x.

DOI:10.1111/j.1745-4603.1971.tb00595.x
PMID:28370123
Abstract

The binding quality of the heat set gel increased when F-actin was present in an appropriate ratio to myosin A. It increased further when tropomyosin was added to the myosin A/F-actin model system. The water holding capacity was increased by tropomyosin only. Thus, the contribution of not only myosin A but also of native tropomyosin and actin should be controlled in sausage manufacture. The presence of 0.6 M NaCl or KCl in the sol was necessary to produce high binding quality and high water holding capacity of heated myosin B gels. NaCl is preferred because of the taste effect on the meat product. Heating temperature (65, 80, or 90°CC) affected the physical properties of heated myosin B gels. The water holding capacity and the maximum relaxation time decreased with increasing temperature. In the manufacture of meat products, the heating temperature should be selected in accordance with the desired properties in the finished product.

摘要

当F-肌动蛋白与肌球蛋白A以适当比例存在时,热凝固凝胶的结合质量会提高。当向肌球蛋白A/F-肌动蛋白模型系统中添加原肌球蛋白时,结合质量会进一步提高。只有原肌球蛋白能提高持水能力。因此,在香肠制作过程中,不仅要控制肌球蛋白A的含量,还要控制天然原肌球蛋白和肌动蛋白的含量。溶胶中存在0.6 M NaCl或KCl对于加热后的肌球蛋白B凝胶产生高结合质量和高持水能力是必要的。由于对肉制品的风味影响,NaCl更为可取。加热温度(65、80或90℃)会影响加热后的肌球蛋白B凝胶的物理性质。持水能力和最大松弛时间随温度升高而降低。在肉制品生产中,应根据成品所需的特性选择加热温度。

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RELATIONSHIPS BETWEEN BINDING QUALITY OF MEAT AND MYOFIBRILLAR PROTEINS: IV. Contribution of Native Tropomyosin and Actin in Myosin B to Rheological Properties of Heat Set Minced-Meat Gel.肉的结合质量与肌原纤维蛋白之间的关系:IV. 肌球蛋白B中天然原肌球蛋白和肌动蛋白对热凝固碎肉凝胶流变学特性的贡献。
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