牛跟腱胶原与草鱼皮胶原的结构表征及自组装行为比较

doi:10.19677/j.issn.1004-7964.2023.01.001

皮革科学与工程 ›› 2023, Vol. 33 ›› Issue (1): 1-8.doi: 10.19677/j.issn.1004-7964.2023.01.001

• 试验研究 • 下一篇

牛跟腱胶原与草鱼皮胶原的结构表征及自组装行为比较

秦子波¹, 余小月¹, 乐薇¹, 荣建华¹, 熊善柏¹, 胡杨^1,2,3,4,*

1.华中农业大学食品科学技术学院,湖北武汉 430070;
2.华中农业大学交叉科学研究院,湖北武汉 430070;
3.国家大宗淡水鱼加工技术研发分中心（武汉）,湖北武汉 430070;
4.华中农业大学深圳营养与健康研究院,湖北武汉 430070

收稿日期:2022-05-20 出版日期:2023-02-01 上线日期:2023-01-04
通讯作者: *胡杨（1987-）,男,副教授,博士生导师,研究方向为水产品加工及副产物高值化利用。E-mail: huyang@mail.hzau.edu.cn。
作者简介:秦子波（1998-）,男,硕士研究生,研究方向为水产品加工及副产物高值化利用。E-mail: qinzibo1998@163.com。
基金资助:
湖北省自然科学基金面上项目（2022CFB162）; 华中农业大学-中国农业科学院深圳农业基因组研究所合作基金(SZYJY2021009); 现代农业产业技术体系专项资金(CARS-45-48)

Comparison of the Structures and Self-assembly Behaviors of Collagens Extracted from Bovine Achilles Tendon and Grass Carp Skin

QIN Zibo¹, YU Xiaoyue¹, YUE Wei¹, RONG Jianhua¹, XIONG Shanbai¹, HU Yang^1,2,3,4,*

1. College of Food Science and Technology, Huazhong Agriculture University, Wuhan 430070, China;
2. Interdisciplinary Sciences Institute, Huazhong Agricultural University, Wuhan 430070, China;
3. The Sub Center (Wuhan) of National Technology and R&D of Staple Freshwater Fish Processing, Wuhan 430070, China;
4. Shenzhen Institute of Nutrition and Health, Huazhong Agricultural University, Wuhan 430070, China

Received:2022-05-20 Online:2023-02-01 Published:2023-01-04

摘要/Abstract

摘要： 以牛跟腱和草鱼皮为原料,采用“酸-酶”结合法提取I型胶原,研究两种胶原的结构特性及其自组装行为差异。结果表明：牛跟腱胶原和草鱼皮胶原均具有I型胶原的典型结构特点,具有相似的相对分子质量和二级结构,但氨基酸含量有所差异,其中牛跟腱胶原亚氨基酸（脯氨酸+胫脯氨酸）含量要高于草鱼皮胶原。胶原的自组装结果表明,当胶原质量浓度为2 mg/mL、温度为37 ℃时胶原自组装速率最高。而当温度过高（>42 ℃）时,相比牛跟腱胶原,草鱼皮胶原的组装受到更大地抑制,这可能归因于牛跟腱胶原中更多的亚氨基酸含量赋予了其更好的热稳定性。此外,增大胶原浓度可以提升胶原凝胶的存储模量,整体而言,牛跟腱胶原凝胶的存储模量优于草鱼皮胶原凝胶。

关键词: 胶原, 结构表征, 自组装, 动力学

Abstract: Type I collagen was separately extracted from bovine achilles tendon and grass carp (Ctenopharyngodon Idella) skin by using the acid-enzyme combination method. The structural properties and self-assembly behavior of the two collagens were investigated. Results showed that both collagens had the typical structural characteristics of type I collagen. The two collagens had similar molecular weight and secondary structure but were different in amino acid contents. The content of imino acids (proline+hydroproline) in bovine achilles tendon collagen was higher than that of grass carp skin collagen. The results of collagen self-assembly experiments showed that the highest self-assembly rate was achieved when the collagen concentration was 2 mg/mL and the temperature was 37 ℃. However, the assembly of collagen from grass carp skin was more inhibited than that of bovine achilles tendon collagen when the temperature was too high (> 42 ℃), which might be attributed to the higher thermal stability of bovine achilles tendon collagen induced by its higher content of imino acids. Besides, the storage modulus of collagen hydrogel was promoted with increasing collagen concentration, and generally collagen hydrogels’ performance derived from bovine achilles tendon was superior to that from grass carp skin.

Key words: collagen, structural characterization, self-assembly, kinetics

中图分类号:

TS512

秦子波, 余小月, 乐薇, 荣建华, 熊善柏, 胡杨. 牛跟腱胶原与草鱼皮胶原的结构表征及自组装行为比较[J]. 皮革科学与工程, 2023, 33(1): 1-8.

QIN Zibo, YU Xiaoyue, YUE Wei, RONG Jianhua, XIONG Shanbai, HU Yang. Comparison of the Structures and Self-assembly Behaviors of Collagens Extracted from Bovine Achilles Tendon and Grass Carp Skin[J]. Leather Science and Engineering, 2023, 33(1): 1-8.

参考文献

[1] Asaduzzaman A K, Getachew A T, Cho Y J, et al.Characterization of pepsin-solubilised collagen recovered from mackerel(Scomber japonicus)bone and skin using subcritical water hydrolysis[J].International Journal of Biological Macromolecules, 2020, 148: 1290-1297.
[2] 么林妍,凌碧扬,刘晓乐,等.非变性牦牛骨胶原蛋白的提取与表征[J].皮革科学与工程,2022,173(1):9-14.
[3] 闫鸣艳. 几种生物大分子对罗非鱼皮Ⅰ型胶原自聚集性的影响[J].食品科学,2017,38(19):24-29.
[4] Zhu S C,Yuan Q J,Yin T,et al.Self-assembly of collagen-based biomaterials:preparation,characterizations and biomedical applications[J].Journal of Materials Chemistry B,2018,6(18):2650-2676.
[5] Liu Y,Ma D,Wang Y,et al.A comparative study of the properties and self-aggregation behavior of collagens from the scales and skin of grass carp(Ctenopharyngodon idella)[J].International Journal of Biological Macromolecules,2018,106:516-522.
[6] Yu X Y,Yuan Q J,Yang M T,et al.Development of biocompatible and antibacterial collagen hydrogels via dialdehyde polysaccharide modification and tetracycline hydrochloride loading[J].Macromolecular Materials and Engineering,2019,304(5):1800755.
[7] 杨波,李国英.牛蛙皮中未变性Ⅰ型胶原蛋白的提取及性能表征[J].皮革科学与工程,2012,117(5):5-8+19.
[8] Wang J, Pei X L, Liu H Y, et al.Extraction and characterization of acid-soluble and pepsin-soluble collagen from skin of loach(Misgurnus anguillicaudatus)[J]. International Journal of Biological Macromolecules, 2018, 106: 544-550.
[9] 周艳华,张鹏飞,李涛,等.干制大鲵皮胶原蛋白提取工艺优化[J].食品工业,2020,41(1):1-4.
[10] Ali A M M,Kishimura H,Benjakul S.Extraction efficiency and characteristics of acid and pepsin soluble collagens from the skin of golden carp(Probarbus Jullieni)as affected by ultrasonication[J].Process biochemistry,2018,66:237-244.
[11] Paola C M,Camila A M,Ana C,et al.Functional textile finishing of type I collagen isolated from bovine bone for potential healthtech[J].Heliyon,2019,5(2):e01260.
[12] 李倩,杨欢,李国英.[EMIM][AC]溶剂对Ⅰ型胶原结构的影响[J].皮革科学与工程,2017,147(5):5-9.
[13] Noorzai S,Verbeek C J R,Lay M C,et al.Collagen extraction from various waste bovine hide sources[J].Waste and Biomass Valorization,2020,11(11):5687-5698.
[14] Asaduzzaman A K M,Getachew A T,Cho Y J,et al.Characterization of pepsin-solubilised collagen recovered from mackerel(Scomber japonicus)bone and skin using subcritical water hydrolysis[J].International Journal of Biological Macromolecules,2020,148:1290-1297.
[15] 瞿怡,苏寒雨,刘文涛,等.超声波辅助法提取牛皮胶原蛋白[J].皮革科学与工程,2018,28(2):5-9.
[16] 李新莹,缪可言,葛黎明,等.胶原蛋白热变性检测方法的比较研究[J].皮革科学与工程,2021,169(3):41-45.
[17] 王璐,但卫华,但年华.胎牛皮源高层级胶原聚集体的制备与表征[J].皮革科学与工程,2019,159(5):16-22.
[18] Zhang J J,Duan R.Characterisation of acid-soluble and pepsin-solubilised collagen from frog(Rana nigromaculata)skin[J].International Journal of Biological Macromolecules,2017,101:638-642.
[19] 兰文婷,金若芸,刘耀文,等.草鱼鳞和草鱼皮胶原蛋白性质及自聚集行为对比研究[J].食品与发酵工业,2018,44(2):92-97.
[20] 赵燕,鲁亮,杨玲,等.草鱼皮胶原的体外自组装动力学研究[J].食品科学,2014,35(11):21-26.
[21] 陈元昊,李冰清,缪楠,等.草鱼皮胶原蛋白的理化性质及其自组装的影响因素分析[J].食品科技,2018,43(9):192-196.
[22] 闫鸣艳,秦松.聚集条件对罗非鱼皮Ⅰ型胶原自聚集动力学的影响[J].食品工业科技,2016,37(2):93-97+102.
[23] 梁艳萍,王艳,汪海波,等.草鱼鱼鳞胶原蛋白体外自组装行为的研究[J].食品科学,2011,32(23):15-20.
[24] 缪楠. 鲫鱼皮胶原蛋白理化性质及其自组装行为研究[D].镇江:江苏科技大学,2019.
[25] 闫婷婷. 胶原自组装行为的研究[D].郑州:郑州大学,2017.
[26] 金达丽. 淡水鱼鳞胶原蛋白的提取及体外自组装性质的研究[D].南昌:江西科技师范大学,2018.
[27] 赵燕,鲁亮,杨玲,等.草鱼和乌鳢鱼皮胶原体外自组装过程中的凝胶化行为比较研究[J].食品科学,2014,35(19):34-38.

牛跟腱胶原与草鱼皮胶原的结构表征及自组装行为比较

Comparison of the Structures and Self-assembly Behaviors of Collagens Extracted from Bovine Achilles Tendon and Grass Carp Skin

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