title: Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins.
abstract: The angiotensin I-converting enzyme (ACE) inhibitory activity of protein hydrolysates from tilapia muscle fractions, namely mince (M), washed mince (WM), and sarcoplasmic protein (SP), were investigated. Each fraction was hydrolyzed by Virgibacillus halodenitrificans SK1-3-7 proteinases for up to 24h. After 8h of hydrolysis, the M hydrolysate (48% degree of hydrolysis (DH)) showed the highest ACE inhibitory activity, with an IC50value of 0.54mg/ml, while the SP hydrolysate exhibited the lowest DH and ACE inhibition. In vitro gastrointestinal digestion reduced the ACE inhibitory activity of the M hydrolysate but enhanced its transport across Caco-2 cell monolayers. The transported peptides were found to contain 3-4 amino acid residues showing strong ACE inhibition. The novel ACE inhibitory peptide with the highest inhibition was found to be MCS, with an IC50value of 0.29μM. Therefore, tilapia mince hydrolyzed by V. halodenitrificans proteinases contained ACE inhibitory peptides that are potentially bioavailable.
authors.affiliation: School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
authors.forename: Tidarat
authors.initials: T
authors.lastname: Toopcham
authors.affiliation: Food & Biobased Research, Wageningen University and Research Centre, Bornse Weilanden 9, P.O. Box 17, 6700 AA Wageningen, The Netherlands.
authors.forename: Jurriaan J
authors.initials: JJ
authors.lastname: Mes
authors.affiliation: Food & Biobased Research, Wageningen University and Research Centre, Bornse Weilanden 9, P.O. Box 17, 6700 AA Wageningen, The Netherlands.
authors.forename: Harry J
authors.initials: HJ
authors.lastname: Wichers
authors.affiliation: National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathum Thani 12120, Thailand.
authors.forename: Sittiruk
authors.initials: S
authors.lastname: Roytrakul
authors.affiliation: School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand. Electronic address: jirawat@sut.ac.th.
authors.forename: Jirawat
authors.initials: J
authors.lastname: Yongsawatdigul
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000818:Animals; D001682:Biological Availability; D018938:Caco-2 Cells; D006801:Humans; D009124:Muscle Proteins / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000494:pharmacology*; D011492:Protein Hydrolysates / Q000494:pharmacology*; D017210:Tilapia; D058679:Virgibacillus / Q000201:enzymology*
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D009124:Muscle Proteins; D010455:Peptides; D011492:Protein Hydrolysates; D010447:Peptide Hydrolases
keywords: ACE inhibitory activity; Caco-2 permeability; Muscle proteins; Protein hydrolysates; Tilapia