Skim milk protein distribution as a result of very high hydrostatic pressure
This work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pressures. The changes found in micellar size correlated with the concentration of soluble casein, because treatments at 250 MPa significantly enhanced the level of non-sedimentable casein while, between 700 and 900 MPa, there were no further increases with respect to lower pressures. There was a severe β-lactoglobulin (β-Lg) denaturation at pressures ≥ 700 MPa, which reached 77–87%. α-Lactalbumin (α-La) was stable up to 550 MPa, but it denatured at higher pressures. The content of soluble lactoferrin (Lf) decreased with pressure, particularly from 550 to 800 MPa, while that of secretory IgA (sIgA) progressively decreased from 250 up to 700 MPa. Our results indicated that treatment of milk at very high pressures, from 700 to 900 MPa, did not reduce micellar size nor released more soluble casein with respect to treatments at lower pressures (250–550 MPa). However, these treatments led to a severe denaturation of the whey proteins, in particular of β-Lg and the minor proteins Lf and sIgA. The possibility of using high hydrostatic pressure to obtain a soluble milk fraction with a casein and whey protein composition similar to that of human milk is discussed.
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Format: | artículo biblioteca |
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Elsevier
2015
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Subjects: | Whey proteins, Very high hydrostatic pressure, Casein, Milk protein distribution, Lactoferrin, Secretory IgA, |
Online Access: | http://hdl.handle.net/10261/149976 |
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dig-cial-es-10261-1499762018-09-20T07:41:27Z Skim milk protein distribution as a result of very high hydrostatic pressure Bravo, Francisca I. Felipe, Xavier López-Fandiño, Rosina Molina, Elena Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA This work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pressures. The changes found in micellar size correlated with the concentration of soluble casein, because treatments at 250 MPa significantly enhanced the level of non-sedimentable casein while, between 700 and 900 MPa, there were no further increases with respect to lower pressures. There was a severe β-lactoglobulin (β-Lg) denaturation at pressures ≥ 700 MPa, which reached 77–87%. α-Lactalbumin (α-La) was stable up to 550 MPa, but it denatured at higher pressures. The content of soluble lactoferrin (Lf) decreased with pressure, particularly from 550 to 800 MPa, while that of secretory IgA (sIgA) progressively decreased from 250 up to 700 MPa. Our results indicated that treatment of milk at very high pressures, from 700 to 900 MPa, did not reduce micellar size nor released more soluble casein with respect to treatments at lower pressures (250–550 MPa). However, these treatments led to a severe denaturation of the whey proteins, in particular of β-Lg and the minor proteins Lf and sIgA. The possibility of using high hydrostatic pressure to obtain a soluble milk fraction with a casein and whey protein composition similar to that of human milk is discussed. This work received financial support from the project CENIT-2007-2016Futural, Ingenio Program. Peer Reviewed 2017-05-19T07:56:12Z 2017-05-19T07:56:12Z 2015 2017-05-19T07:56:12Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.foodres.2015.03.014 issn: 0963-9969 e-issn: 1873-7145 Food Research International 72: 74-79 (2015) http://hdl.handle.net/10261/149976 10.1016/j.foodres.2015.03.014 Sí none Elsevier |
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Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA |
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Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA Bravo, Francisca I. Felipe, Xavier López-Fandiño, Rosina Molina, Elena Skim milk protein distribution as a result of very high hydrostatic pressure |
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This work studies the micellar size and the distribution of caseins, major and minor whey proteins in different fractions of skim milk treated up to 900 MPa for 5 min. Transmission electron microscopy showed that the smallest casein micelles were formed around 450 MPa with no variations at higher pressures. The changes found in micellar size correlated with the concentration of soluble casein, because treatments at 250 MPa significantly enhanced the level of non-sedimentable casein while, between 700 and 900 MPa, there were no further increases with respect to lower pressures. There was a severe β-lactoglobulin (β-Lg) denaturation at pressures ≥ 700 MPa, which reached 77–87%. α-Lactalbumin (α-La) was stable up to 550 MPa, but it denatured at higher pressures. The content of soluble lactoferrin (Lf) decreased with pressure, particularly from 550 to 800 MPa, while that of secretory IgA (sIgA) progressively decreased from 250 up to 700 MPa. Our results indicated that treatment of milk at very high pressures, from 700 to 900 MPa, did not reduce micellar size nor released more soluble casein with respect to treatments at lower pressures (250–550 MPa). However, these treatments led to a severe denaturation of the whey proteins, in particular of β-Lg and the minor proteins Lf and sIgA. The possibility of using high hydrostatic pressure to obtain a soluble milk fraction with a casein and whey protein composition similar to that of human milk is discussed. |
format |
artículo |
topic_facet |
Whey proteins Very high hydrostatic pressure Casein Milk protein distribution Lactoferrin Secretory IgA |
author |
Bravo, Francisca I. Felipe, Xavier López-Fandiño, Rosina Molina, Elena |
author_facet |
Bravo, Francisca I. Felipe, Xavier López-Fandiño, Rosina Molina, Elena |
author_sort |
Bravo, Francisca I. |
title |
Skim milk protein distribution as a result of very high hydrostatic pressure |
title_short |
Skim milk protein distribution as a result of very high hydrostatic pressure |
title_full |
Skim milk protein distribution as a result of very high hydrostatic pressure |
title_fullStr |
Skim milk protein distribution as a result of very high hydrostatic pressure |
title_full_unstemmed |
Skim milk protein distribution as a result of very high hydrostatic pressure |
title_sort |
skim milk protein distribution as a result of very high hydrostatic pressure |
publisher |
Elsevier |
publishDate |
2015 |
url |
http://hdl.handle.net/10261/149976 |
work_keys_str_mv |
AT bravofranciscai skimmilkproteindistributionasaresultofveryhighhydrostaticpressure AT felipexavier skimmilkproteindistributionasaresultofveryhighhydrostaticpressure AT lopezfandinorosina skimmilkproteindistributionasaresultofveryhighhydrostaticpressure AT molinaelena skimmilkproteindistributionasaresultofveryhighhydrostaticpressure |
_version_ |
1777671250063130624 |