@article{ZHANG2024, 
author = {Chuhan ZHANG and Yinge CHEN and Ting MA and Ling WENG and Lingjing ZHANG and Genfang ZHANG and Minjie CAO},
title = {Preparation and Purification of Dipeptidyl Peptidase-Ⅳ Inhibitory Peptides from Pearl Mussel Muscle},
year = {2024},
journal = {Food Science},
volume = {45},
number = {17},
pages = {63-70},
keywords = {pearl mussel, enzymatic hydrolysis, separation and purification, dipeptidyl peptidase-Ⅳ, inhibitory peptides},
url = {https://www.sciopen.com/article/10.7506/spkx1002-6630-20240125-233},
doi = {10.7506/spkx1002-6630-20240125-233},
abstract = {ObjectiveBioactive peptides with an inhibitory effect on dipeptidyl peptidase-Ⅳ (DPP-Ⅳ) were prepared from pearl mussel muscle.MethodsTwo-step enzymatic hydrolysis was adopted and enzymatic hydrolysis conditions were optimized. Fractions with in vitro DPP-Ⅳ inhibitory activity were concentrated by ultrafiltration, and purified by SuperdexTM peptide 10/300 GL gel filtration column chromatography and reverse phase-high performance liquid chromatography (RP-HPLC). DPP-Ⅳ inhibitory peptides were purified from the enzymatic hydrolysate and their amino acid sequences were identified by liquid chromatography-tandem mass spectrometry.ResultsBoth neutral protease and alkaline protease could effectively hydrolyze pearl mussel muscle. After concentration using a 3 kDa cut-off ultrafiltration membrane, the DPP-Ⅳ inhibition rate of the enzymatic hydrolysate reached 67.4%. After separation by gel filtration column and purification by RP-HPLC, 6 active peptides were obtained, whose sequences were FNAPAM, FIPNY, IYNPPTPF, LAMPYP, FFVVMP and LAGMP, respectively. Furthermore, the interactions between these peptides and DPP-Ⅳ were analyzed by molecular docking.ConclusionOur present study provides a theoretical reference for the effective utilization of fish processing byproducts as raw materials for functional food production.}
}