Rapid screening, identification and inhibition mechanism of α-glucosidase inhibitory peptide from hemp seed

  • LI Zhuoying ,
  • LIU Jingxing ,
  • LIAO Dankui ,
  • LI Weiguo ,
  • LAN Xiongdiao ,
  • LIU Pengru
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  • 1(School of Chemistry and Chemical Engineering, Guangxi Minzu University, Guangxi Key Laboratory for Polysaccharide Materials and Modification, Institute of Chemical and Biological Transformation Processes, Nanning 530006, China)
    2(Hunan Light-Textile Industrial Design Institute CO.Ltd., Changsha 410015, China)
    3(School of Chemistry and Chemical Engineering, Guangxi University, Guangxi Key Laboratory of Petrochemical Resource Processing and Process Intensification Technology, Nanning 530004, China)
    4(Key Laboratory of Pesticide Development and Application Technology of Guangxi Ministry of Agriculture and Rural Affairs, Key Laboratory of High Efficiency Pesticide and Application Technology of Guangxi, Guangxi Tianyuan Biochemical Co.Ltd., Nanning 530007, China)

Received date: 2025-02-17

  Revised date: 2025-03-13

  Online published: 2025-12-15

Abstract

Hemp seed protein was hydrolyzed by bromelain.Taking the α-glucosidase inhibitory rate as the evaluation metrics as the evaluation index, the enzymatic hydrolysis conditions were optimized through single-factor and orthogonal experiments, and the optimal enzymatic hydrolysis conditions were established as follows:the pH value for enzymatic hydrolysis was 8.0, the enzymolysis temperature was 45 ℃, the ratio of bromelain to protein was 6 000 U/g, and the enzymatic hydrolysis time was 0.5 h.Under these conditions, the semi-inhibitory concentration (IC50) of the enzymatic hydrolysate against α-glucosidase was (2.65±0.063) mg/mL.Ultrafiltration was carried out on the enzymatic hydrolysate to collect fractions less than 10 kDa.Then, the biological composite material 3-MPBA/AG@aZIF-7/PDA was used for affinity purification.Subsequently, through LC-MC/MC mass spectrometry and computer virtual screening, five novel polypeptides with potential hypoglycemic activity (KFL, KFY, SLFK, SWG, and YFK) were obtained.In vitro experiments and molecular docking studies showed that KFY had the best activity [(IC50 was (3.10±0.22) mmol/L], and all five peptides could form hydrogen bonds and hydrophobic interactions with the amino acid residues on α-glucosidase, thereby binding to α-glucosidase and forming a stable complex.This study provides theoretical basis and data support for the high-value utilization of hemp seed protein and also provides reference for the screening of natural hypoglycemic drugs.

Cite this article

LI Zhuoying , LIU Jingxing , LIAO Dankui , LI Weiguo , LAN Xiongdiao , LIU Pengru . Rapid screening, identification and inhibition mechanism of α-glucosidase inhibitory peptide from hemp seed[J]. Food and Fermentation Industries, 2025 , 51(22) : 264 -271 . DOI: 10.13995/j.cnki.11-1802/ts.042380

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