Distribution, Typical Structure and Self-Assembly Properties of Collagen from Fish Skin and Bone

Xuening Zhang; Jie Wang; Qian Zhang; Yan Fan; Hongwei Zhang; Khurshid Ahmad; Hu Hou

doi:10.3390/molecules28186529

Distribution, Typical Structure and Self-Assembly Properties of Collagen from Fish Skin and Bone

Molecules. 2023 Sep 8;28(18):6529. doi: 10.3390/molecules28186529.

Authors

Xuening Zhang¹, Jie Wang¹, Qian Zhang¹, Yan Fan², Hongwei Zhang³, Khurshid Ahmad¹, Hu Hou^{1

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Affiliations

¹ College of Food Science and Engineering, Ocean University of China, Sansha Road, Qingdao 266404, China.
² College of Marine Life Sciences, Ocean University of China, Yushan Road, Qingdao 266003, China.
³ Technology Center of Qingdao Customs, Xinyue Road, Qingdao 266109, China.
⁴ Laboratory for Marine Drugs and Bioproducts, Laoshan Laboratory, Qingdao 266237, China.
⁵ Sanya Oceanographic Institution, Ocean University of China, Sanya 572024, China.
⁶ Qingdao Institute of Marine Bioresources for Nutrition and Health Innovation, Qingdao 266000, China.

Abstract

The source and type of collagen are crucial to its application, and both play a decisive role. Collagen was prepared from both tilapia skin and bone and skate skin and cartilage, named as CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c, respectively. Types, distributions, structures, and self-assembly of collagen were studied. It showed that yellow collagen fibers from skin arranged longitudinally, while collagen fibers from skate cartilages displayed varying colors. CI-TI-s, CI-TI-b, CI-SK-s, and CII-SK-c showed the typical amide A (3316-3336 cm^-1) and amide B (2929-2948 cm^-1) in FTIR spectra. CI-TI-b and CII-SK-c showed 218-229 nm of UV absorption, 11.56-12.20 Å of d values in XRD, and 0.12-0.14 of Rpn values in CD. The thermal denaturation temperatures of CI-TI-s and CI-SK-s were 30.7 and 20.6 °C, respectively. The self-assembly of CI-TI-s and CII-SK-c were maximum at pH 7.2 and 7.4-7.6, respectively. The unique collagen peptides of tilapia and skate were GPSGPQGAVGATGPK, PAMPVPGPMGPMGPR, SPAMPVPGPMGPMGPR, GESGPSGPAGPAGPAGVR, SSGPPVPGPIGPMGPR, GLTGPIGVPGPPGAQGEK, GLAGPQGPR, and GLSGDPGVQGIK, respectively. The unique peptides of type I and type II collagen were GPTGEIGATGLAGAR, GVLGLTGMR, LGLTGMR, GEPGAAGPAGPSGPMGPR, SSGPPVPGPIGPMGPR, and GLSGDPGVQGIK, respectively.

Keywords: collagen; self-assembly; structure; unique peptide.

MeSH terms

Animals
Collagen Type II
Collagen* / chemistry
Skin / chemistry
Tilapia*

Substances

Collagen
Collagen Type II

Grants and funding

This research was funded by Major Scientific and Technological Innovation Project in Shandong Province, grant number No. 2022CXGC020414; Major Scientific and Technological Innovation Project of Qingdao West Coast New Area, grant number No. ZDKC-2022-01; Taishan Scholar Foundation of Shandong Province, grant number No. tsqn202103033; Marine S&T Fund of Shandong Province for Qingdao Marine Science and Technology Center, grant number No. 2022QNLM030002-4.