Isolation, Purification and Structural Identification of Peptides with Hypolipidemic Activity Derived from Hazelnut Protein

doi:10.7506/spkx1002-6630-20180606-077

Abstract

Abstract: A peptide with higher hypolipidemic activity was separated and purified from the alcalase hydrolysate of hazelnut protein isolate by ultrafiltration, Sephadex G-25 chromatography, Sephadex G-15 chromatography and reversed-phase highperformance liquid chromatography (RP-HPLC). The amino acid sequence of the peptide was identified by Q Exactive hybrid quadrupole-Orbitrap mass spectrometry. The levels of lipid accumulation, total cholesterol, and triglyceride in 3T3-L1 preadipocytes incubated with the peptide were also determined. The results showed that fraction C3 isolated by Sephadex G-15 chromatography had significantly higher inhibitory activity against pancreatic lipase, cholesterol micelle adsorption capacity, and cellular hypolipidemic activity than any other fractions. The peptide was identified as Phe-Leu-Leu-Pro-His (FLLPH), and it could inhibit 26.31% of total lipid accumulation in 3T3-L1 preadipocytes, and reduce cholesterol and triglyceride levels by 32.67% and 23.87%, respectively, compared to the model control. The present study provides a theoretical basis for the development of hypolipidemic peptides from hazelnut protein.

Key words: hypolipidemic peptides, isolation and purification, structural identification, 3T3-L1 preadipocytes

CLC Number:

TS209

ZHOU Meihan, GUO Yong, WEI Zhen, ZHAO Lan, QIN Hanxiong, WANG Ji, MIN Weihong. Isolation, Purification and Structural Identification of Peptides with Hypolipidemic Activity Derived from Hazelnut Protein[J]. FOOD SCIENCE, 2019, 40(16): 124-129.

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Isolation, Purification and Structural Identification of Peptides with Hypolipidemic Activity Derived from Hazelnut Protein

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