000119642 001__ 119642
000119642 005__ 20221115154451.0
000119642 0247_ $$2doi$$a10.3168/jds.2015-9403
000119642 0248_ $$2sideral$$a90902
000119642 037__ $$aART-2015-90902
000119642 041__ $$aeng
000119642 100__ $$aNavarro, F.
000119642 245__ $$aKinetic and thermodynamic parameters for thermal denaturation of ovine milk lactoferrin determined by its loss of immunoreactivity
000119642 260__ $$c2015
000119642 5060_ $$aAccess copy available to the general public$$fUnrestricted
000119642 5203_ $$aLactoferrin is a protein with important biological functions that can be obtained from milk and by-products derived from the dairy industry, such as whey. Although bovine lactoferrin has been extensively studied, ovine lactoferrin is not quite as well known. In the present study, the effect of several heat treatments in 3 different media, over a temperature range from 66 to 75°C, has been studied on lactoferrin isolated from
sheep milk. Denaturation of lactoferrin was determined by measuring its immunoreactivity with specific polyclonal antibodies. Kinetic and thermodynamic parameters obtained indicate that lactoferrin denatures by
heat more rapidly in whey than in phosphate buffer or milk. The value of activation energy found for the denaturation process of lactoferrin when treated in whey is higher (390 kJ/mol) than that obtained in milk
(194 kJ/mol) or phosphate buffer (179 kJ/mol). This indicates that a great amount of energy is necessary to start denaturation of ovine lactoferrin, probably due to the interaction of this protein with other whey proteins.
The changes in the hydrophobicity of lactoferrin after heat treatments were determined by fluorescence measurement using acrylamide. The decrease in the hydrophobicity constant was very small for the treatments
from 66 to 75°C, up to 20 min, which indicates that lactoferrin conformation did not experienced a greatchange. The results obtained in this study permit the prediction of behavior of ovine lactoferrin under several heat treatments and show that high-temperature, short-time pasteurization (72°C, 15 s) does not cause loss of its immunoreactivity and, consequently, would not affect its conformation and biological activity.
000119642 536__ $$9info:eu-repo/grantAgreement/ES/CICYT/AGL2010-20835
000119642 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000119642 590__ $$a2.408$$b2015
000119642 591__ $$aFOOD SCIENCE & TECHNOLOGY$$b28 / 125 = 0.224$$c2015$$dQ1$$eT1
000119642 591__ $$aAGRICULTURE, DAIRY & ANIMAL SCIENCE$$b3 / 58 = 0.052$$c2015$$dQ1$$eT1
000119642 592__ $$a1.479$$b2015
000119642 593__ $$aAnimal Science and Zoology$$c2015$$dQ1
000119642 593__ $$aFood Science$$c2015$$dQ1
000119642 593__ $$aGenetics$$c2015$$dQ2
000119642 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000119642 700__ $$aHarouna, S.$$uUniversidad de Zaragoza
000119642 700__ $$0(orcid)0000-0001-5373-9210$$aCalvo, M.$$uUniversidad de Zaragoza
000119642 700__ $$0(orcid)0000-0003-2555-8425$$aPérez, M. D.$$uUniversidad de Zaragoza
000119642 700__ $$0(orcid)0000-0001-5964-823X$$aSánchez, L.$$uUniversidad de Zaragoza
000119642 7102_ $$12008$$2780$$aUniversidad de Zaragoza$$bDpto. Produc.Animal Cienc.Ali.$$cÁrea Tecnología de Alimentos
000119642 773__ $$g98, 7 (2015), 4328-4337$$pJ. dairy sci.$$tJournal of Dairy Science$$x0022-0302
000119642 8564_ $$s1091724$$uhttps://zaguan.unizar.es/record/119642/files/texto_completo.pdf$$yVersión publicada
000119642 8564_ $$s3087325$$uhttps://zaguan.unizar.es/record/119642/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000119642 909CO $$ooai:zaguan.unizar.es:119642$$particulos$$pdriver
000119642 951__ $$a2022-11-15-12:12:04
000119642 980__ $$aARTICLE