title: Recovery, viscoelastic and functional properties of Barbel skin gelatine: investigation of anti-DPP-IV and anti-prolyl endopeptidase activities of generated gelatine polypeptides.
abstract: The characteristics and functional properties of gelatine from freshwater fish skin (Barbus callensis) were investigated. The gelatine extraction efficiency was improved by an acid-swelling process in the presence of barbel crude acid protease extract. Barbel skin gelatine (BSG) contained 92.15% protein, 0.31% lipid and 0.72% ash. The amino acid profile of BSG showed a high percentage of imino acids. The electrophoretic profile showed that BSG is mainly composed of α- and β-components. BSG showed an excellent solubility and possessed interfacial properties, which were governed by the protein concentration. Biological activities of the hydrolysates obtained after digestion of BSG with several commercial proteases were evaluated. The results suggested that these hydrolysates are a good source of natural inhibitors of dipeptidyl peptidase-IV and prolyl endopeptidase and could potentially be used as dietary ingredients in the management of type 2-diabetes and/or neuropathological disorders.
authors.affiliation: Unité Enzyme et Bioconversion, ENIS, University of Sfax, Tunisia.
authors.forename: Assaâd
authors.initials: A
authors.lastname: Sila
authors.affiliation: Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Madrid, Spain.
authors.forename: Oscar
authors.initials: O
authors.lastname: Martinez-Alvarez
authors.affiliation: Faculty of Sciences of Gabes, University of Gabes, Tunisia.
authors.forename: Anissa
authors.initials: A
authors.lastname: Haddar
authors.affiliation: Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Madrid, Spain.
authors.forename: M Carmen
authors.initials: MC
authors.lastname: Gómez-Guillén
authors.affiliation: Laboratory of Microbiology and Enzyme Engineering, ENIS, University of Sfax, Tunisia.
authors.forename: Moncef
authors.initials: M
authors.lastname: Nasri
authors.affiliation: Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Madrid, Spain.
authors.forename: M Pilar
authors.initials: MP
authors.lastname: Montero
authors.affiliation: Higher Institute of Biotechnology of Sfax, PB 1175, 3038 Sfax, Tunisia. Electronic address: ali.bougatef79@gmail.com.
authors.forename: Ali
authors.initials: A
authors.lastname: Bougatef
mesh_terms: D000818:Animals; D003530:Cyprinidae / Q000378:metabolism; D003924:Diabetes Mellitus, Type 2 / Q000188:drug therapy; D018819:Dipeptidyl Peptidase 4 / Q000378:metabolism; D054873:Dipeptidyl-Peptidase IV Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D005780:Gelatin / Q000737:chemistry* / Q000302:isolation & purification; D006868:Hydrolysis; D019636:Neurodegenerative Diseases / Q000188:drug therapy; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D012867:Skin / Q000737:chemistry; D012995:Solubility; D055682:Viscoelastic Substances / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D054873:Dipeptidyl-Peptidase IV Inhibitors; D010455:Peptides; D015842:Serine Proteinase Inhibitors; D055682:Viscoelastic Substances; D005780:Gelatin; D018819:Dipeptidyl Peptidase 4; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases
keywords: Dipeptidyl peptidase-IV; Freshwater fish; Gelatine; Hydrolysates; Prolyl endopeptidase