title: Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate.
abstract: The impact of enzymatic hydrolysis by Alcalase on the conformational and functional properties of chickpea protein isolate (CPI) was investigated. The physicochemical, interfacial tension and surface characteristics of CPI and their hydrolysates (CPH) according to the degree of hydrolysis (DH) were also determined. These parameters were then related to the changes in the emulsification activity (EAI) and stability (ESI). The enzymatic hydrolysis was found to improve protein recovery and solubility, leading to a reduction in the molecular weight bands with a concomitant increase in the intensity and appearance of protein bands having apparent molecular mass below 20 kDa. The interfacial tension decreased from ∼ 66.5 mN m(-1) for CPI to ∼ 59.1 m Nm(-1) for CPH. A similar trend was observed for the surface charge which declined from -27.55 mV to -16.4 mV for the CPI and CPH, respectively. These changes were found to have a detrimental effect on the EAI and ESI values.
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Laboratoire Analyse, Valorisation et Sécurité des Aliments, Route de Soukra, 3038 Sfax, Tunisia.
authors.forename: Abir
authors.initials: A
authors.lastname: Mokni Ghribi
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Laboratoire Analyse, Valorisation et Sécurité des Aliments, Route de Soukra, 3038 Sfax, Tunisia.
authors.forename: Ines
authors.initials: I
authors.lastname: Maklouf Gafsi
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Unité Enzymes et Bioconversion, route de Soukra, 3038 Sfax, Tunisia; Institut Régional de Recherche en Agroalimentaire et Biotechnologie: Charles Viollette, EA1026, Equipe ProBioGEM, Université Lille 1, France.
authors.forename: Assaâd
authors.initials: A
authors.lastname: Sila
authors.affiliation: Université de Liège, Gembloux Agro Bio-Tech, Unité de Technologie des Industries Agro-Alimentaires, passage des Déportés 2, 5030 Gembloux, Belgium.
authors.forename: Christophe
authors.initials: C
authors.lastname: Blecker
authors.affiliation: Université de Liège, Gembloux Agro Bio-Tech, Unité de Technologie des Industries Agro-Alimentaires, passage des Déportés 2, 5030 Gembloux, Belgium.
authors.forename: Sabine
authors.initials: S
authors.lastname: Danthine
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Laboratoire Analyse, Valorisation et Sécurité des Aliments, Route de Soukra, 3038 Sfax, Tunisia.
authors.forename: Hamadi
authors.initials: H
authors.lastname: Attia
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Unité Enzymes et Bioconversion, route de Soukra, 3038 Sfax, Tunisia.
authors.forename: Ali
authors.initials: A
authors.lastname: Bougatef
authors.affiliation: Université de Sfax, Ecole Nationale d'Ingénieurs de Sfax, Laboratoire Analyse, Valorisation et Sécurité des Aliments, Route de Soukra, 3038 Sfax, Tunisia. Electronic address: besbes.s@voila.fr.
authors.forename: Souhail
authors.initials: S
authors.lastname: Besbes
mesh_terms: D002152:Calorimetry, Differential Scanning; D055598:Chemical Phenomena; D029863:Cicer / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011492:Protein Hydrolysates / Q000737:chemistry; D012995:Solubility; D013381:Subtilisins / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D011492:Protein Hydrolysates; D013381:Subtilisins
keywords: Chickpea protein isolates; Conformation; Enzymatic hydrolysis; Functional properties