Phaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestine

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cg.creator.identifierStephen E Beebe: 0000-0002-3742-9930en
cg.identifier.doihttps://doi.org/10.1017/s0007114507819179en
cg.isijournalISI Journalen
cg.issn1475-2662en
cg.issue3en
cg.journalBritish Journal of Nutritionen
cg.reviewStatusPeer Reviewen
cg.subject.ciatBEANSen
cg.subject.ciatNUTRITIONen
cg.volume99en
dc.contributor.authorMontoya Marmolejo, Carlos Aníbalen
dc.contributor.authorLeterme, Pen
dc.contributor.authorBeebe, Stephen E.en
dc.contributor.authorSouffrant, WBen
dc.contributor.authorMolle, Den
dc.contributor.authorLalles, JPen
dc.date.accessioned2014-10-02T08:32:59Zen
dc.date.available2014-10-02T08:32:59Zen
dc.identifier.urihttps://hdl.handle.net/10568/43941
dc.titlePhaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestineen
dcterms.abstractThe study aimed to investigate the in vivo digestion of Phaseolus vulgaris phaseolin types differing in their subunit pattern composition. Diets contained either casein as the sole source of protein or a mixture (1:1) of casein and pure Sanilac (S), Tendergreen (T) or Inca (I) phaseolin either unheated or heated. Rats were fed for 11 d with the experimental diets. Their ileal content and mucosa were collected and prepared for electrophoresis, Western blotting, densitometry and MS. Differences in digestion among native phaseolin types were observed for intact phaseolin at molecular weights (MW) of 47 50·5 kDa and for an undigested fragment at MW of 19 21·5 kDa in ileal digesta. In both cases, the concentration of these protein bands was lower for I phaseolin than for S or T phaseolin (P < 0·05). In the mucosa, the concentration of a protein band at MW of 20·5 21·5 kDa was lower for S phaseolin as compared to T or I phaseolin (P < 0·001). The presence of phaseolin subunits and their fragments was confirmed by Western blotting. MS analysis revealed the presence of undigested ? and ? subunit fragments from phaseolin and endogenous proteins (anionic trypsin I and pancreatic ?-amylase) in ileal digesta. Thermal treatment improved digestion (P < 0·01), acting on both dietary and endogenous protein components. In conclusion, this study provides evidence for differences in intestinal digestion among phaseolin types, S phaseolin being more resistant and I phaseolin more susceptible. These differences were affected by the origin of the phaseolin subunit precursor. Heat treatment enhanced phaseolin digestion.en
dcterms.accessRightsOpen Accessen
dcterms.available2008-03-01en
dcterms.bibliographicCitationMontoya Marmolejo, Carlos Aníbal; Leterme, Pascal; Beebe, Stephen E.; Souffrant, Wolfgang B.; Mollé, Daniel; Lalles, Jean-Paul. 2008. Phaseolin type and heat treatment influence the biochemistry of protein digestion in the rat intestine . British Journal of Nutrition 99:531-539.en
dcterms.extentp. 531-539en
dcterms.issued2008-03en
dcterms.languageenen
dcterms.licenseCopyrighted; all rights reserveden
dcterms.publisherCambridge University Pressen
dcterms.subjectphaseolus vulgarisen
dcterms.subjectglobulinsen
dcterms.subjectdigestionen
dcterms.subjectnutritive valueen
dcterms.subjectglobulinasen
dcterms.subjectdigestiónen
dcterms.subjectvalor nutritivoen
dcterms.typeJournal Articleen

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