This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-solu...This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-soluble(albumin),salt-soluble(globulin),alkaline-soluble(glutelin)and ethanol-soluble(prolamin).Globulin was the most abundant fraction,consisting of 91%protein,followed by glutelin,albumin and prolamin in decreasing order.Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed polypeptides of sizes≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19,85 and 100 kDa.Prolamin had polypeptide sizes 20,40 and 100 kDa.The albumin and globulin fractions had higher intrinsic fluorescence intensity(FI)values than the glutelin.Albumin had a higher solubility(ranging from 80 to 100%)over a wide pH range when compared with the other fractions.Water holding capacity(g/g)reduced from 2.76(glutelin)to 1.35(prolamin)followed by 0.42(globulin)and 0.08(albumin).Oil holding capacity(g/g)reduced from:4.13(glutelin)to 2.57(globulin)and 1.56,1.50 for albumin and prolamin respectively.Gelling ability was stronger for prolamin and glutelin than albumin and globulin,while higher emulsion(p<0.05)quality was obtained for prolamin and albumin than for glutelin and globulin.展开更多
基金Natural Sciences and Engineering Research Council of Canada(NSERC),funding reference number RGPIN 2018–06019Cette recherche aétéfinancée par le Conseil de recherches en sciences naturelles et en génie du Canada(CRSNG),numéro de référence RGPIN 2018–06019.
文摘This work evaluated the functional properties of sesame protein fractions in order to determine their potential in food applications.Sesame seed protein fractions were prepared according to their solubility:water-soluble(albumin),salt-soluble(globulin),alkaline-soluble(glutelin)and ethanol-soluble(prolamin).Globulin was the most abundant fraction,consisting of 91%protein,followed by glutelin,albumin and prolamin in decreasing order.Non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)showed polypeptides of sizes≥20 kDa for albumin while glutelin and globulin had similar polypeptide sizes at 19,85 and 100 kDa.Prolamin had polypeptide sizes 20,40 and 100 kDa.The albumin and globulin fractions had higher intrinsic fluorescence intensity(FI)values than the glutelin.Albumin had a higher solubility(ranging from 80 to 100%)over a wide pH range when compared with the other fractions.Water holding capacity(g/g)reduced from 2.76(glutelin)to 1.35(prolamin)followed by 0.42(globulin)and 0.08(albumin).Oil holding capacity(g/g)reduced from:4.13(glutelin)to 2.57(globulin)and 1.56,1.50 for albumin and prolamin respectively.Gelling ability was stronger for prolamin and glutelin than albumin and globulin,while higher emulsion(p<0.05)quality was obtained for prolamin and albumin than for glutelin and globulin.
