王 柯,郭志文,段 蕊,周天宇,张俊杰.水产胶原蛋白热稳定性与环境温度相关性研究进展[J].食品安全质量检测学报,2024,15(2):251-257
水产胶原蛋白热稳定性与环境温度相关性研究进展
Research progress on correlation between thermal stability of aquatic collagen and environmental temperature
投稿时间:2023-12-07  修订日期:2024-01-18
DOI:
中文关键词:  胶原蛋白  热稳定性  三螺旋结构  亚基  环境温度
英文关键词:collagen  thermal stability  triple helix structure  subunit  environmental temperature
基金项目:江苏省高等学校重点发展计划(PAPD);江苏省大学生创新创业培训计划(SY202111641638009)
作者单位
王 柯 江苏海洋大学海洋食品与生物工程学院 
郭志文 江苏海洋大学海洋科学与水产学院 
段 蕊 江苏海洋大学海洋科学与水产学院 
周天宇 江苏海洋大学海洋食品与生物工程学院 
张俊杰 江苏海洋大学海洋食品与生物工程学院 
AuthorInstitution
WANG Ke College of Ocean Food and Biological Engineering, Jiangsu Ocean University 
GUO Zhi-Wen College of Marine Science and Fisheries, Jiangsu Ocean University 
DUAN Rui College of Marine Science and Fisheries, Jiangsu Ocean University 
ZHOU Tian-Yu College of Ocean Food and Biological Engineering, Jiangsu Ocean University 
ZHANG Jun-Jie College of Ocean Food and Biological Engineering, Jiangsu Ocean University 
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中文摘要:
      水产胶原蛋白是一种优良的生物材料, 被广泛应用于医药、化妆品、食品加工等领域。但水产胶原蛋白热稳定性较差, 且目前对其热稳定性与环境温度相关性的研究较少。本文详细论述水产胶原蛋白的三螺旋结构, 对其热稳定性的来源作出详细分析, 并以环境温度为主导因素, 综述生存环境温度差异带来的水产胶原蛋白氨基酸组成变化、结构变化(亚基组成, 翻译后修饰)与热稳定性差异。生存在较高温度下的生物, 其胶原的变性温度(denaturation temperature, Td)也相对较高, 且含有较高比例的α1亚基与较少的α2、α3亚基, 反之亦然。这种亚基比例改变的实质可能涉及Ⅰ型胶原α1(I)α2(I)α3(I)与α1(I)2α2(I)分子构型的互相转变。除上述变化, 变温动物可以调节胶原翻译后修饰数量, 辅助亚基比例的变化, 增强或降低胶原的热稳定性, 这是变温动物特有的一种能力。水产胶原蛋白的热稳定性随环境温度的变化而改变, 是生物对环境适应能力的一部分。本文对现阶段关于胶原蛋白结构、热稳定性与环境温度相关性的研究进行总结, 以期为胶原蛋白材料的研究与应用提供参考。
英文摘要:
      Aquatic collagen is an excellent biological material, widely used in medicine, cosmetics, food processing and other fields. However, the thermal stability of aquatic collagen is poor and few studies have been conducted to correlate its thermal stability with the environmental temperature. This paper discussed the triple helix structure of aquatic collagen in detail, analyzed the sources of its thermal stability in detail, and reviewed the changes in aquatic collagen amino acid composition, structure (subunit composition, post-translational modification) and thermal stability caused by the difference in living environmental temperature. Organisms living at higher temperatures had a relatively high denaturation temperature (Td) of collagen, and contained a higher proportion of α1 and less α2 and α3, and vice versa. The substance of this change in subunit ratio might involve the interconversion between the molecular configuration of type Ⅰ collagen α1(I)2α2(I) and α1(I)α2(I)α3(I) molecular configurations. In addition to the above changes, poikilotherms could adjust the amount of post-translational modification of collagen, as a complement to changes in subunit proportions, and enhanced or decreased the thermal stability of collagen, which was a unique ability of poikilotherms. The thermal stability of aquatic collagen changes with the change of environmental temperature, which was part of the adaptability of organisms to the environment. This paper summarized the current state of research on the structure, thermal stability and environmental temperature correlation of aquatic collagen to provide a reference for research and application of aquatic collagen materials.
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