Novel Se-enriched α-glucosidase inhibitory peptide derived from tuna dark meat: Preparation, identification and effects on IR-HepG2 cells

被引:3
|
作者
Yu, Hui [1 ]
Xian, Meiting [1 ]
Qu, Caiye [1 ]
Peng, Pai [1 ]
Yongo, Edwine [2 ]
Guo, Zhiqiang [3 ]
Du, Zhixun [4 ]
Xiao, Juan [1 ,5 ]
机构
[1] Hainan Univ, Hainan Engn Res Ctr Aquat Resources Efficient Util, Sch Food Sci & Engn, Key Lab Seafood Proc Haikou, Haikou 570228, Peoples R China
[2] Hainan Univ, Sch Life Sci, Haikou 570228, Peoples R China
[3] Hainan Univ, Sch Marine Sci & Engn, Haikou 570228, Peoples R China
[4] SCNU, Int Dept, Affiliated High Sch, Guangzhou 510635, Peoples R China
[5] Hainan Univ, Sch Food Sci & Engn, 58 Renmin Ave, Haikou 570228, Peoples R China
关键词
Tuna dark meat; Se-enriched peptides; alpha-glucosidase; T2DM; IR-HepG2; cells; BIOACTIVE PEPTIDES; SELENIUM;
D O I
10.1016/j.fbio.2024.104357
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Se -enriched peptides serve various physiological functions and are crucial sources of Se. This study found the Se content of yellowfin tuna dark meat was 18.34 mg/kg (dry weight), making it an ideal natural source of Seenriched peptides. We used five different enzymatic treatments to prepare Se -enriched protein hydrolysates from dark meat. Among them, the trypsin-generated protein hydrolysate showed the highest alpha-glucosidase inhibition activity. It was then fractionated by ultrafiltration followed by RP-HPLC, and the sequences of Seenriched peptide obtained were identified from the most active fraction by LC-MS/MS. Subsequently, KPLSeCPK was screened by in silico analyses and validated by the alpha-glucosidase activity inhibition experiment (IC 50 = 0.828 mM). Molecular docking and inhibition kinetics assay further demonstrated the interaction between KPLSeCPK and alpha-glucosidase, suggesting its potential as a novel hyperglycemic inhibitor. Moreover, KPLSeCPK lessened IR and boosted antioxidant capability of IR-HepG2 cells. Thus, KPLSeCPK provides a valuable reference for efficiently utilizing natural organic Se.
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页数:11
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