Purification and identification of a novel antidiabetic peptide from Chinese giant salamander (Andrias davidianus) protein hydrolysate against α-amylase and α-glucosidase

ABSTRACT

This study aimed to purify and identify a novel antidiabetic peptides from Chinese giant salamander (Andrias davidianus) protein hydrolysate and to evaluate its anti-diabetic properties against α-amylase and α-glucosidase. The isolation was done by gel filtration, reverse phase chromatography (RF-HLPC), and finally peptide and amino acid sequences were identified by LC/MS/MS system. Our results revealed five novel peptides that strongly inhibited α-amylase and α-glucosidase. The peptides’ amino acid sequences were Cys-Ser-Ser-Val (MW = 393.99 Da), Tyr-Ser-Phe-Arg (MW = 570.99 Da), Ser-Ala-Ala-Pro (MW = 343.89 Da), Pro-Gly-Gly-Pro (MW = 325.99 Da) and Leu-Gly-Gly-Gly-Asn (MW = 415.99 Da) possessing α-amylase inhibitory activity IC₅₀ of 13.76 × 10³, 10.82 × 10³, 4.46 × 10³, 4.23 × 10³, and 2.86 × 10³ µg/mL, respectively; and for α-glucosidase with IC₅₀ of 206.00, 162.00, 66.90, 63.50, and 42.93 µg/mL, respectively. Intriguingly, the peptide LGGGN showed higher inhibition on both α-amylase and α-glucosidase and could be considered as a potential anti-diabetic inhibitor.

KEYWORDS:

• Anti-diabetic peptide
• Chinese giant salamander
• LC/MS/MS
• Protein hydrolysates
• RP-HPLC
• α-amylase
• α-glucosidase

Declaration of interest

Authors declare that they have no conflict of interest.

Additional information

Funding

We thank Natural Science Foundation of Jiangsu Province (BK20150152) for their financial support under program of “Collaborative innovation center of food safety and quality control in Jiangsu We declare that this manuscript is from our original finding and has not been previously published, is not currently submitted for publication to any other journal, and will not be submitted elsewhere before a decision is made by this journal and the provided data are from original finding of our research.