Volume 19 Issue 3
Jun.  2023
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HUO Yumei, HU Xiao, WU Yanyan, JIANG Jinjin. Preparation, separation and physicochemical properties of α-glucosidase inhibitory peptides from Miichthys miiuy[J]. South China Fisheries Science, 2023, 19(3): 98-109. DOI: 10.12131/20220269
Citation: HUO Yumei, HU Xiao, WU Yanyan, JIANG Jinjin. Preparation, separation and physicochemical properties of α-glucosidase inhibitory peptides from Miichthys miiuy[J]. South China Fisheries Science, 2023, 19(3): 98-109. DOI: 10.12131/20220269
shu

Preparation, separation and physicochemical properties of α-glucosidase inhibitory peptides from Miichthys miiuy

  • 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.

    Department of Food, Guangzhou City Polutechnic, Guangzhou 510405, China

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  • Received Date: October 10, 2022
  • Revised Date: December 18, 2022
  • Accepted Date: December 21, 2022
  • Available Online: December 26, 2022
    Graphical Abstract
    • Abstract
  • In order to achieve the high-value utilization of Miichthys miiuy processing by-products, taking α-glucosidase inhibition rate as an index, we carried out a single factor experiment and applied the response surface methodology to optimize the preparation process of α-glucosidase inhibitory peptides from minced fish muscle of M. miiuy processing by-products. The optimal enzymatic hydrolysis conditions with trypsin were as follows: hydrolysis time 4.8 h, enzyme dosage 0.21%, hydrolysis pH 8.5, material-liquid ratio 1∶2 (m/V), hydrolysis temperature 46 ℃. On this basis, we analyzed the inhibitory activity of the enzymatic hydrolysates before and after the simulated gastrointestinal digestion in vitro, and drew the kinetic curve of enzyme inhibition. Then we separated the enzymatic hydrolysate by SephadexG-25 so as to investigate the molecular weight distribution and amino acid composition of the enzymatic hydrolysates. The results show that the α-glucosidase inhibitory rate increased to 61.79% after that the α-glucosidase inhibitory peptide was simulated gastrointestinal digestion in vitro. Its inhibition type on α-glucosidase was mixed type inhibition. The molecular mass of the enzymatic hydrolysate was concentrated below 3 kD, accounting for 91.85%. After the separation by G-25, the α-glucosidase inhibition rate of F4 fraction was 58.05%. In Group F4, 78.28% of peptides were less than 1 kD. The amino acid analysis shows that the enzymatic hydrolysate was rich in Asp, Glu, Arg, Tyr, Val, Ala, Leu and Lys.
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