Screening and identification of high bioavailable oligopeptides from rapeseed napin (Brassica napus) protein-derived hydrolysates via Caco-2/HepG2 co-culture model. (May 2022)

• Record Type: Journal Article
• Authors: Yao, Meng; Yao, Yijun; Qin, Bowen; Pan, Mengmeng; Ju, Xingrong; Xu, Feiran; Wang, Lifeng
• Is Part Of: Food research international. Volume 155(2022)
• Publication Date: 2022-05
• Subjects: A novel digestive device -- Absorbable compositions -- Antidiabete -- GLUT4 expression and translocation -- In vitro -- LC-ESI-QTOF-MS; GLUT4 Glucose transporter 4 -- Papp Apparent permeability coefficient -- RNPHs Rapeseed napin protein-derived hydrolysates -- IR Insulin resistance -- DH Degree of hydrolysis -- T2DM Type 2 diabetes mellitus -- PI3K Phosphatidylinositol kinase -- AKT Protein Kinase B -- ACN Acetonitrile -- OPA Ortho-phthaldialdehyde -- TFA Trifluoroacetic acid -- HBSS Hank's balanced salt solution -- DMEM Dulbecco's modified eagle's medium -- FBS Fetal bovine serum -- PBS Phosphate buffer saline -- BSA Bovine serum albumin -- DMSO Dimethyl sulfoxide -- MTT 3-(4, 5-dimethylthiazol-2-yl)-2, 5diphenyltetrazolium bromide -- ECL Electrochemiluminescence -- AAG Amino acid groups -- SEC-HPLC High-performance size-exclusion chromatography -- Mw Molecular-weight -- Mr Molecular -- OD Optical density -- LC-ESI-QTOF-MS Liquid chromatography coupled with electrospray ionisation and quadrupole time of flight tandem mass spectrometry -- TIC Total ion current -- RT Retention time -- UniProtKB UniProt Knowledgebase -- IPI Ile-Pro-Ile -- VPL Val-Pro-Leu -- IPQVS Ile-Pro-Gln-Val-Ser -- THLPK Thr-His-Leu-Pro-Lys -- HLPK His-Leu-Pro-Lys -- (I) LPK (Ile)Leu-Pro-Lys -- HLK His-Leu-Lys -- LHK Leu-His-Lys -- LK Leu-Lys -- MQ Met-Gln -- NPQ Asn-Pro-Gln -- QR Gln-Arg -- LLQ Leu-Leu-Gln -- TLK Thr-Leu-Lys -- SK Ser-Lys -- VK Val-Lys -- VR Val-Arg -- GQ Gly-Gln -- SR Ser-Arg -- YR Tyr-Arg -- CR Cys-Arg -- RK Arg-Lys -- HK His-Lys -- HKQ His-Lys-Gln -- QQR Gln-Gln-Arg -- PTLK Pro-Thr-Leu-Lys -- GASK Gly-Ala-Ser-Lys -- AVK Ala-Val-Lys -- KAVK Lys-Ala-Val-Lys -- QLQ Gln-Leu-Gln; Food -- Analysis -- Periodicals; Food industry and trade -- Periodicals; Food industry and trade -- Canada -- Periodicals; Food Technology -- Periodicals; Food -- Periodicals; Food-Processing Industry -- Periodicals; Aliments -- Industrie et commerce -- Périodiques; Aliments -- Industrie et commerce -- Canada -- Périodiques; Aliments -- Recherche -- Périodiques; Food industry and trade; Canada; Periodicals; Electronic journals; 664.005
• DOI: 10.1016/j.foodres.2022.111101
• Languages: English
• ISSNs: 0963-9969

Abstract

Graphical abstract: Highlights: A novel digestive device was combined with ultrasound-assisted enzyme hydrolysis. The DH of napin is positively correlated with GLUT4 expression and translocation. The Caco-2/HepG2 co-culture model was used to screen anti-diabetic oligopeptides. High bioavailable oligopeptides were identified from both RNPHs −1 and RNPH-2. Abstract: Rapeseed napin ( Brassica napus ) protein-derived hydrolysates (RNPHs, 1–4) are mixtures of peptides, prior to reaching liver tissue and playing their antidiabetic role, at least being absorbed and metabolized by the intestinal barrier. The study aims at screening and identifying high bioavailable rapessed napin-derived oligopeptides via simulated gastrointestinal digestion and absorption. Specifically, RNPHs were obtained using a novel ultrasound-assisted digestive device. The potential capacity of treating type 2 diabetes mellitus (T2DM) was evaluated preliminarily via enhancing glucose transporter 4 (GLUT4) expression and translocation. Also, absorbable rapeseed napin-derived oligopeptides were screened and identified in a Caco-2/HepG2 co-culture model using liquid chromatography coupled with electrospray ionisation and quadrupole time of flight tandem mass spectrometry (LC-ESI-QTOF-MS). The results involved mainly two aspects. First, absorbable oligopeptides from RNPH-1 (Molecular weight, Mw ≤ 3 kDa) with the highest degree of hydrolysis (DH) were the optimal ones to enhance GLUT4 expression and translocation ( P < 0.05). Secondly, oligopeptides (Thr-His-Leu-Pro-Lys (THLPK), His-Leu-Pro-Lys (HLPK), (Ile) Leu-Pro-Lys ((I)LPK), His-Leu-Lys (HLK), and Leu-His-Lys (LHK)), identified from both RNPH-1 and RNPH-2 which significantly enhanced GLUT4 expression and translocation, could be absorbed intact and reached HepG2 cells. These findings indicated that high bioavailable oligopeptides from RNPHs were the potential usefulness to treat T2DM in vitro .