FURTHER-STUDIES ON THE ROLES OF THE HEAD AND TAIL REGIONS OF THE MYOSIN MOLECULE IN HEAT-INDUCED GELATION
FURTHER-STUDIES ON THE ROLES OF THE HEAD AND TAIL REGIONS OF THE MYOSIN MOLECULE IN HEAT-INDUCED GELATION
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DOI：
10.1111/j.1365-2621.1982.tb11040.x
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发表时间：
1982-01-01
影响因子：
3.9
通讯作者：
YASUI, T
中科院分区：
文献类型：
--
作者：
ISHIOROSHI, M;SAMEJIMA, K;YASUI, T
通过带式粘度计中的刚性测量和使用扫描电子显微镜的直接检查，研究了肌球蛋白的 2 种蛋白水解片段（重（HMM）和轻肌球蛋白（LMM））的热诱导凝胶化特性。在 pH 6.0 的 0.6 M KCl 中发现了 LMM 和 HMM 的热诱导网络形成能力。 LMM 产生的凝胶对应于 40-70°C 温度范围内的可逆螺旋-螺旋转变。 C，根据系统浊度变化评估，几乎没有聚集的证据。 HMM 在 pH 5.0 和盐浓度 0.1 M 时不可逆地产生刚性增加的凝胶。SH 基团的氧化似乎仅涉及 LMM，而不涉及 HMM 凝胶化过程。 [这项研究涉及肉类加工]。
Heat induced gelation properties of the 2 proteolytic fragments of myosin, heavy (HMM) and light meromyosin (LMM), were studied by rigidity measurement in a band type viscometer and by a direct examination using a scanning electron microscope. A heat induced network forming abilty for LMM and HMM was found in 0.6 M KCl at a pH 6.0. LMM produced gels corresponding to a reversible helix-coil transition at temperatures ranging from 40-70.degree. C, with little evidence of aggregation as assessed from a turbidity change of the system. HMM associated irreversibly producing a gel with increased rigidity at pH 5.0 and a salt concentration of 0.1 M. Oxidation of SH-groups appeared to be involved only in LMM and not in HMM gelation process. [This study relates to meat processing].