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dc.contributor.authorHoz, Lucia de la; et al.-
dc.contributor.otherPT_Br
dc.date.accessioned-
dc.date.accessioned2022-09-30T19:25:43Z-
dc.date.availablePT_Br
dc.date.available2022-09-30T19:25:43Z-
dc.date.copyright-
dc.date.issued2014-
dc.identifierPT_Br
dc.identifier.citationFood Chemistry, London, v. 142, n. 1, p.166-169, jan. 2014.pt_BR
dc.identifier.urihttp://repositorio.ital.sp.gov.br/jspui/handle/123456789/479-
dc.description.abstractThe extract of sugar-cane yeast (Saccharomyces cerevisiae) was enzymatically hydrolysed by Alcalase, Protex or Viscozyme. Hydrolysates were fractionated using a membrane ultrafiltration system and peptides smaller than 5 kDa were evaluated for iron chelating ability through measurements of iron solubility, binding capacity and dialyzability. Iron-chelating peptides were isolated using immobilized metal affinity chromatography (IMAC). They showed higher content of His, Lys, and Arg than the original hydrolysates. In spite of poor iron solubility, hydrolysates of Viscozyme provided higher iron dialyzability than those of other enzymes. This means that more chelates of iron or complexes were formed and these kept the iron stable during simulated gastro-intestinal digestion in vitro, improving its dialyzability.pt_BR
dc.formatPT_Br
dc.languagePT_Br
dc.language.isoenpt_BR
dc.publisherElsevierpt_BR
dc.rightsPT_Br
dc.sourcePT_Br
dc.subjectSugar-cane yeastpt_BR
dc.subjectIron-chelating peptidespt_BR
dc.subjectDialyzabilitypt_BR
dc.subjectImmobilized metal affinity chromatographypt_BR
dc.titleIron-binding properties of sugar cane yeast peptidespt_BR
dc.typeArticlept_BR
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