Enhanced hydrophobic interaction between fish (Cyprinus carpio L.) scale gelatin and curcumin: Mechanism study

Li H 1 , Wan Mustapha WA 2 , Tian G 3 , Dong N 4 , Zhao F 5 , Zhang X 5 Show all authors , Long D 6 , Liu J 7

Affiliations 

  • 1 The Key Laboratory of Environmental Pollution Monitoring and Disease Control, Ministry of Education, Guizhou Provincial Engineering Research Center of Ecological Food Innovation, School of Public Health, Guizhou Medical University, Guiyang 550025, China; Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia (UKM), Bangi 43600, Malaysia
  • 2 Department of Food Sciences, Faculty of Science and Technology, Universiti Kebangsaan Malaysia (UKM), Bangi 43600, Malaysia
  • 3 School of Liquor & Food Engineering, Guizhou University, Guiyang 550025, China
  • 4 Institute of Food Processing Technology, Guizhou Academy of Agricultural Sciences, Guiyang 550006, China
  • 5 Guizhou Fishery Research Institute, Guizhou Academy of Agricultural Science, Guiyang 550025, China
  • 6 Chongqing Vocational Institute of Safety & Technology, Chongqing 404121, China
  • 7 The Key Laboratory of Environmental Pollution Monitoring and Disease Control, Ministry of Education, Guizhou Provincial Engineering Research Center of Ecological Food Innovation, School of Public Health, Guizhou Medical University, Guiyang 550025, China; School of Liquor & Food Engineering, Guizhou University, Guiyang 550025, China; Institute of Food Processing Technology, Guizhou Academy of Agricultural Sciences, Guiyang 550006, China. Electronic address: mcgrady456@163.com
Food Chem, 2024 Jan 15;431:137102.
PMID: 37579608 DOI: 10.1016/j.foodchem.2023.137102

Abstract

To enhance the solubility of hydrophobic nutrients, the hydrophobicity of fish scale gelatin hydrolysate (FSGH) was increased with moderate acid or alkali hydrolysis. Acid-induced FSG hydrolysate (AcFSGH) at 3 h showed a superior curcumin loading efficiency (18.30 ± 0.38 μg/mL) among all FSGHs. Compared with FSG, the proportion of hydrophobic amino acids (from 41.1% to 46.4%) and the hydrophobic interaction (from 12.72 to 20.10 mg/mL) was significantly increased in the AcFSGH. Meanwhile, the transformation of the α-helix (from 12.8% to 4.9%) to the β-sheet (from 29.0% to 42.8%) was also observed in the AcFSGH. Based on the observation in the molecular weight and morphological analysis, AcFSGH acquired the best hydrophobic interaction with curcumin, presumably due to the formation of the flexible structure of the linear hydrolyzates. The above results call for an investigation of the role of FSG hydrolysate in the synthesis of nanoparticles loaded with bioactive lipophilic compounds.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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