Ultrasonic-assisted Extraction and Structure Characterization of Collagen from Camel Skin

被引：0
|
作者：
Shi R. [1 ]
He J. [1 ]
Jirimutu [1 ,2 ]
机构：
[1] College of Food Science and Engineering, Inner Mongolia Agriculture University, Hohhot
[2] Camel Research Institute of Inner Mongolia, Alex
来源：
Journal of Chinese Institute of Food Science and Technology | 2022年 / 22卷 / 02期
关键词：
Camel skin; Collagen; Response surface methodology; Structure characterization; Ultrasonic-assisted extraction;
D O I：
10.16429/j.1009-7848.2022.02.023
中图分类号：
学科分类号：
摘要：
The objective of this study was to obtain the optimal technology of ultrasonic-assisted extraction of collagen from camel skin, and the extracted collagen was characterized and analyzed. In the experiment, the extraction rate of collagen was used as an indicator to explore the effects of enzyme loading, solid-liquid ratio, ultrasonic power, ultrasonic treatment time and total extraction time on camel skin collagen. After determining the ultrasonic power, on the basis of one-factor-at-a-time method, combined with response surface analysis, the best extraction conditions: enzyme loading of 4.5%, solid-liquid ratio of 1:23, ultrasonic treatment time of 20 min, total extraction time of 51 h, and the actual extraction rate of collagen was (41.99±1.57) %. The SDS-PAGE analysis suggested that the extracted collagen contained three characteristic chains of type I collagen. Ultraviolet spectroscopy analysis was further inferred to be a typical type I collagen. The Fourier transform infrared spectroscopy analysis confirmed that collagen had a complete triple helix structure. Scanning electron microscopy observation revealed that the extracted collagen was in the form of fibrous with intertwined structure. Meanwhile, the Zeta potential of pH 2~9 of collagen was measured, and the potential value showed a downward trend in this range. The isoelectric point was 6.7. © 2022, Editorial Office of Journal of CIFST. All right reserved.
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页码：213 / 223
页数：10
相关论文
共 28 条
  • [1] SORUSHANOVA A, DELGADO L M, WU Z, Et al., The collagen suprafamily: From biosynthesis to advanced biomaterial development, Advanced Materials (Deerfield Beach, Fla.), 31, 1, (2019)
  • [2] RAMSHAW J A M., Biomedical applications of collagens, Journal of Biomedical Materials Research. Part B, Applied Biomaterials, 104, 4, pp. 665-675, (2016)
  • [3] SINTHUSAMRAN S, BENJAKUL S, KISHIMURA H., Comparative study on molecular characteristics of acid soluble collagens from skin and swim bladder of seabass(Lates calcarifer), Food Chemistry, 138, 4, pp. 2435-2441, (2013)
  • [4] BAI H Y, KE L F., Research progress of collagen application, Journal of Jilin Medical College, 34, 2, pp. 133-135, (2013)
  • [5] SONG H D, ZHANG L, LUO Y K, Et al., Effects of collagen peptides intake on skin ageing and platelet release in chronologically aged mice revealed by cytokine array analysis, Journal of Cellular and Molecular Medicine, 22, 1, pp. 277-288, (2018)
  • [6] SIONKOWSKA A, SKRZYNSKI S, SMIECHOWSKI K, Et al., The review of versatile application of collagen, Polymers for Advanced Technologies, 28, 1, pp. 4-9, (2017)
  • [7] DILAN RASIKA D M, SENAKA RANADHEERA C, IDANARACHCHI J K V., Applications of marine-derived peptides and proteins in the food industry, Marine Proteins and Peptides, pp. 545-587, (2013)
  • [8] SIM OES G S, SILVEIRA E T F, DE OLIVEIRA S R, Et al., Optimum conditions for extracting collagen from the tunica albuginea of immunologically castrated pig testes and the functional properties of the isolated collagen, Meat Science, 96, 4, pp. 1460-1468, (2014)
  • [9] CHANG X H, ZHANG M X, LU R, Et al., Study on the tissue structure of camel skin in China, China Leather, 1, pp. 6-8, (1986)
  • [10] GAO L L, HOU C L, GAO Y, Et al., Research advances of thermal stability of collagen, Journal of Chinese Institute of Food Science and Technology, 18, 5, pp. 200-212, (2018)
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