Volume 19 Issue 1
Feb.  2023
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SONG Yuqiong, HU Xiao, XIANG Huan, CHEN Shengjun, LI Laihao, YANG Xianqing, WU Yanyan, MA Haixia. Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides[J]. South China Fisheries Science, 2023, 19(1): 155-164. DOI: 10.12131/20220097
Citation: SONG Yuqiong, HU Xiao, XIANG Huan, CHEN Shengjun, LI Laihao, YANG Xianqing, WU Yanyan, MA Haixia. Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides[J]. South China Fisheries Science, 2023, 19(1): 155-164. DOI: 10.12131/20220097
shu

Study on tyrosinase inhibitory activity and Cu2+ binding activity of tilapia skin peptides

  • 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.

    Dalian Polytechnic University/Collaborative Innovation Center of Provincial and Ministerial Co-Construction for Marine Food Deep Processing, Dalian 116034, China

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  • Received Date: April 06, 2022
  • Revised Date: June 05, 2022
  • Accepted Date: July 18, 2022
  • Available Online: July 25, 2022
    Graphical Abstract
    • Abstract
  • To find out whether the tilapia (Oreochromis) skin collagen peptides can effectively inhibit melanin production, we used enzymatic method to prepare the tilapia skin tyrosinase (TYR) inhibitory peptides (TSTIP) and studied the relevance between TYR inhibitory activity and Cu2+ binding activity. The results show that the product of tilapia skin hydrolyzed by alcalase for 4 h exhibited both the highest TYR inhibitory activity and Cu2+ binding activity, which were significantly positively correlated (R=0.856). When TSTIP was bound to Cu2+ or tyrosinase, the intrinsic fluorescence absorption had a consistent decreasing trend, but the UV absorption increased and the maximum absorption wavelength had a red shift. For FTIR results, TYR and Cu2+ bound to TSTIP mainly by carbonyl and amino groups. Circular dichroism shows that the β-turn and random curl contents of the two conjugates decreased relatively, while the β-fold content increased relatively, which was more obvious for TSTIP-Cu2+ conjugate. In conclusion, the structural change of TSTIP-TYR is similar with that of TSTIP-Cu2+ conjugate, which indicates that TSTIP can inhibit TYR's activity by binding to its Cu2+ active site.
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    • References (36)
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