Volume 20 Issue 2
Apr.  2024
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LU Chen, HU Xiao, CHEN Shengjun, WU Yanyan, HUANG Hui, XIANG Huan, QI Bo, DENG Jianchao. Preparation, in vitro activity and physicochemical properties of collagenase inhibitory peptide from tilapia skin[J]. South China Fisheries Science, 2024, 20(2): 150-159. DOI: 10.12131/20230205
Citation: LU Chen, HU Xiao, CHEN Shengjun, WU Yanyan, HUANG Hui, XIANG Huan, QI Bo, DENG Jianchao. Preparation, in vitro activity and physicochemical properties of collagenase inhibitory peptide from tilapia skin[J]. South China Fisheries Science, 2024, 20(2): 150-159. DOI: 10.12131/20230205
shu

Preparation, in vitro activity and physicochemical properties of collagenase inhibitory peptide from tilapia skin

  • 1.

    College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China

  • 2.

    South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences/Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, Guangzhou 510300, China

  • 3.

    Sanya Tropical Fisheries Research Institute, Sanya 572000, Hainan

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  • Received Date: October 25, 2023
  • Revised Date: December 19, 2023
  • Accepted Date: January 29, 2024
  • Available Online: February 04, 2024
    Graphical Abstract
    • Abstract

  • Tilapia skin, rich in collagen, is an ideal raw material for preparation of bioactive peptides. To provide references for the high-value utilization of tilapia processing by-products and the development of food protein-derived collagenase inhibitors, we prepared tilapia skin collagenase inhibitory peptide (TSCIP) from tilapia skin by enzymatic hydrolysis, and studied the correlation between its collagenase inhibitory activity and metal ion binding activity. The results show that the tilapia skin product hydrolyzed by alkaline protease for 4 h had the highest collagenase inhibition activity, as well as Zn2+ and Mg2+ binding activity, and it was mainly composed of small molecular peptides (<1 000 D accounting for 85.65%). Ultraviolet (UV), Fourier transform infrared (FTIR) and circular dichroism (CD) analysis show that the secondary structure of TSCIP changed after binding with Zn2+, Mg2+ and collagenase, and the β-sheet content of TSCIP increased significantly. Zn2+ and Mg2+ bind to TSCIP mainly through carboxyl oxygen, amino nitrogen atoms and carbonyl groups, while collagenase binds to TSCIP mainly through amino nitrogen atoms and carbonyl groups.

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    • References (38)
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