A calorimetric study of thermal denaturation of recombinant human lactoferrin from rice
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Date
2007-06-13
Authors
Conesa Montanel, CeliaSánchez, Lourdes
Pérez, Maria Dolores
Calvo, Miguel
Journal Title
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Publisher
American Chemical Society
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texto , revista , artículo , artículo originalAbstract
Thermal 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.
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Bibliographic citation
Conesa, 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
AGROVOC subjects
LactoferrinaProteína de cereales
Calorimetría diferencial de barrido
Estabilidad
Arroz
Transgenesis