A calorimetric study of thermal denaturation of recombinant human lactoferrin from rice

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dc.contributor.authorConesa Montanel, Celia
dc.contributor.authorSánchez, Lourdes
dc.contributor.authorPérez, Maria Dolores
dc.contributor.authorCalvo, Miguel
dc.contributor.orcidConesa Montanel, Celia [0000-0003-0862-9893]
dc.date.accessioned2025-12-20T07:14:04Z
dc.date.available2025-12-20T07:14:04Z
dc.date.issued2007-06-13
dc.date.updated2025-12-18T12:50:49Z
dc.description.abstractThermal denaturation of recombinant human lactoferrin from transgenic rice with different degrees of iron saturation has been studied by differential scanning calorimetry. The maximum temperature, enthalpy change, and activation energy of denaturation were higher when recombinant lactoferrin was more saturated with iron, indicating an increase in the stability of the protein structure. Maximum temperature and activation energy values for apo- and holo-lactoferrins were practically identical to those reported for the same forms of lactoferrin from human milk, which indicates a similar thermal stability. However, the value of enthalpy change for denaturation of the recombinant lactoferrin was 2.5-3-fold lower than that found for the human milk protein. This finding may reflect the influence that the different glycosylation pattern may have in the relationship between lactoferrin domains. Denaturation of recombinant lactoferrin in milk was compared with denaturation in phosphate buffer, and results indicated that the protein was more heat-sensitive when treated in milk than in buffer.
dc.description.peerreviewedSi
dc.identifier.citationConesa, C., Sánchez, L., Pérez, M.-D., & Calvo, M. (2007). A Calorimetric Study of Thermal Denaturation of Recombinant Human Lactoferrin from Rice. Journal of Agricultural and Food Chemistry, 55(12), 4848-4853. https://doi.org/10.1021/jf063335u
dc.identifier.issn0021-8561
dc.identifier.issn10.1021/jf063335u
dc.identifier.urihttps://doi.org/10.1021/jf063335u
dc.identifier.urihttps://hdl.handle.net/10532/8063
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.relation.citaSi
dc.relation.publisherversionhttps://doi.org/10.1021/jf063335u
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spainen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subject.agrovocLactoferrina
dc.subject.agrovocProteína de cereales
dc.subject.agrovocCalorimetría diferencial de barrido
dc.subject.agrovocEstabilidad
dc.subject.agrovocArroz
dc.subject.agrovocTransgenesis
dc.subject.sdgHambre cero
dc.subject.sdgSalud y bienestar
dc.titleA calorimetric study of thermal denaturation of recombinant human lactoferrin from rice
dc.typetexto
dc.typerevista
dc.typeartículo
dc.typeartículo original
dc.type.hasVersionversión sometida a revisión

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