Please use this identifier to cite or link to this item: http://ri.uaemex.mx/handle20.500.11799/67607
DC FieldValueLanguage
dc.creatorERIK ALPIZAR REYES-
dc.creatorJohanna Castaño-
dc.creatorHECTOR CARRILLO NAVAS-
dc.creatorRAMIRO JOSE ALVAREZ RAMIREZ-
dc.creatorRaquel Gallardo Rivera-
dc.creatorCESAR PEREZ ALONSO-
dc.creatorANDREA YAZMIN GUADARRAMA LEZAMA-
dc.date2017-08-02-
dc.date.accessioned2022-04-21T05:16:19Z-
dc.date.available2022-04-21T05:16:19Z-
dc.identifierhttp://hdl.handle.net/20.500.11799/67607-
dc.identifier.urihttp://ri.uaemex.mx/handle20.500.11799/67607-
dc.descriptionSe realizó un análisis termodinámico de la proteína de haba liofilizada, para encontrar las mejores condiciones de estabilidad-
dc.descriptionFreeze-dried faba bean (Vicia faba L.) protein adsorption isotherms were determined at 25, 35 and 40 °C and fitted with the Guggenheim-Anderson-de Boer model. The pore radius of protein was in the range of 0.87 to 6.44 nm, so that they were considered as micropores and mesopores. The minimum integral entropy ranged between 4.33 and 4.44 kg H2O/100 kg d.s., was regarded as the point of maximum of stability. The glass transition temperature of the protein equilibrated at the different conditions of storage was determined, showing that the protein remained in glassy state for all cases. The protein showed compact and rigid structures, evidenced by microscopy analysis.-
dc.languageeng-
dc.publisherSpringer-
dc.relation01;01-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0-
dc.source0975-8402-
dc.subjectThermodynamic sorption-
dc.subjectFaba bean-
dc.subjectProtein-
dc.subjectinfo:eu-repo/classification/cti/2-
dc.titleThermodynamic sorption analysis and glass transition temperature of faba bean (Vicia faba L.) protein-
dc.typearticle-
dc.audiencestudents-
dc.audienceresearchers-
item.grantfulltextnone-
item.fulltextNo Fulltext-
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