FOOD SCIENCE ›› 2021, Vol. 42 ›› Issue (10): 120-126.doi: 10.7506/spkx1002-6630-20200226-294

• Bioengineering • Previous Articles     Next Articles

Preparation and Activity Analysis of DPP-IV Inhibitory Peptides from Pacific Oyster (Crassostrea gigas)

CHEN Hong, ZHANG Qian, CHEN Yulei, WENG Ling, ZHANG Lingjing, XIE Shaohao, LIU Guangming, CAO Minjie   

  1. (1. College of Food and Biological Engineering, Jimei University, Xiamen 361021, China;2. Collaborative Innovation Center of Marine Food Deep Processing, Dalian Polytechnic University, Dalian 116034, China)
  • Online:2021-05-25 Published:2021-06-02

Abstract: To prepare dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides, Pacific oyster flesh (Crassostrea gigas) was hydrolyzed with five different proteases, including papain, alcalase, pancreatin, neutrase and protromex. The pancreatin hydrolysate was found to have higher DPP-IV inhibitory activity as compared with the other four hydrolysates. The optimal hydrolysis conditions with pancreatin were determined to be 0.8%, 8.0, 37 ℃ and 90 min for enzyme dosage, pH, temperature, and hydrolysis duration, respectively. The hydrolysate obtained using the optimized conditions was purified and fractionated sequentially by ultrafiltration, Sephadex G-15 column chromatography and high performance liquid chromatography (HPLC) into different peptide fractions. Two DPP-IV inhibitory peptides were obtained and identified as Glu-Ile-Thr-Ala-Leu-Ala-Pro-Ser-Thr-Met-Lys (EITALAPSTMK) and Ile-Leu-Ala-Pro-Pro-Glu-Arg (ILAPPER) by mass spectrometry (MS). Their digestibility characteristics in gastrointestinal fluid were analyzed using online simulation with BIOPEP. Two peptides APSTM and ILAPPER were synthesized by solid-phase synthesis for DPP-IV inhibitory activity evaluation. The results showed that the half-maximal inhibitory concentration (IC50) values of the two peptides were 354.81 and 16.98 mmol/L, respectively. Molecular docking results indicated that inhibitory peptides interacted with the active site of DPP-IV through hydrogen bonds, van der Waals forces and p bonds. The results of this study provide a theoretical basis for the development of functional foods from oyster in the future.

Key words: oyster; dipeptidyl peptidase-IV inhibitory peptide; isolation and purification; inhibitory activity; molecular docking

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