Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin

L. G. Mendoza-Sánchez; M. Jiménez-Fernández; G. Melgar-Lalanne; G. F. Gutiérrez-Lopez; F. Reyes-Espinosa; A. Hernández-Arana; H. Hernández Sánchez

doi:10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/Mendoza

Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin

Translated title of the contribution: Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin

L. G. Mendoza-Sánchez, M. Jiménez-Fernández, G. Melgar-Lalanne, G. F. Gutiérrez-Lopez, F. Reyes-Espinosa, A. Hernández-Arana, H. Hernández Sánchez

Escuela Nacional de Ciencias Biológicas (ENCB)

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Bovine α-lactalbumin (α-LA) was enzymatically modified with a lipase from Rhizopus orizae in an organic environment which catalyzed the covalent bonding of different length chain fatty acids, at reaction times of 3 and 7 days. Structural changes and functional properties of native and enzymatically modified α-LA in a pH range from 3 to 10 were analyzed. The degree of modification was higher than 40 %. The enzymatic lipophilization modified the functionality of the α-LA due to the increase in the surface hydrophobicity. In general, the surface properties were improved by the lipophilization specially at alkaline pH values, increasing the emulsifying activity more than 60 % and showing higher foam stability.

Translated title of the contribution	Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin
Original language	English
Pages (from-to)	331-347
Number of pages	17
Journal	Revista Mexicana de Ingeniera Quimica
Volume	17
Issue number	1
DOIs	https://doi.org/10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/Mendoza
State	Published - 1 Jan 2018

Keywords

Foaming
Functional properties
Lipase
Lipophilization
α-lactalbumin

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10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/Mendoza

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Mendoza-Sánchez, L. G., Jiménez-Fernández, M., Melgar-Lalanne, G., Gutiérrez-Lopez, G. F., Reyes-Espinosa, F., Hernández-Arana, A., & Hernández Sánchez, H. (2018). Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin. Revista Mexicana de Ingeniera Quimica, 17(1), 331-347. https://doi.org/10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/Mendoza

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abstract = "Bovine α-lactalbumin (α-LA) was enzymatically modified with a lipase from Rhizopus orizae in an organic environment which catalyzed the covalent bonding of different length chain fatty acids, at reaction times of 3 and 7 days. Structural changes and functional properties of native and enzymatically modified α-LA in a pH range from 3 to 10 were analyzed. The degree of modification was higher than 40 %. The enzymatic lipophilization modified the functionality of the α-LA due to the increase in the surface hydrophobicity. In general, the surface properties were improved by the lipophilization specially at alkaline pH values, increasing the emulsifying activity more than 60 % and showing higher foam stability.",

keywords = "Foaming, Functional properties, Lipase, Lipophilization, α-lactalbumin",

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Mendoza-Sánchez, LG, Jiménez-Fernández, M, Melgar-Lalanne, G, Gutiérrez-Lopez, GF, Reyes-Espinosa, F, Hernández-Arana, A & Hernández Sánchez, H 2018, 'Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin', Revista Mexicana de Ingeniera Quimica, vol. 17, no. 1, pp. 331-347. https://doi.org/10.24275/uam/izt/dcbi/revmexingquim/2018v17n1/Mendoza

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AU - Mendoza-Sánchez, L. G.

AU - Jiménez-Fernández, M.

AU - Melgar-Lalanne, G.

AU - Gutiérrez-Lopez, G. F.

AU - Reyes-Espinosa, F.

AU - Hernández-Arana, A.

AU - Hernández Sánchez, H.

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N2 - Bovine α-lactalbumin (α-LA) was enzymatically modified with a lipase from Rhizopus orizae in an organic environment which catalyzed the covalent bonding of different length chain fatty acids, at reaction times of 3 and 7 days. Structural changes and functional properties of native and enzymatically modified α-LA in a pH range from 3 to 10 were analyzed. The degree of modification was higher than 40 %. The enzymatic lipophilization modified the functionality of the α-LA due to the increase in the surface hydrophobicity. In general, the surface properties were improved by the lipophilization specially at alkaline pH values, increasing the emulsifying activity more than 60 % and showing higher foam stability.

AB - Bovine α-lactalbumin (α-LA) was enzymatically modified with a lipase from Rhizopus orizae in an organic environment which catalyzed the covalent bonding of different length chain fatty acids, at reaction times of 3 and 7 days. Structural changes and functional properties of native and enzymatically modified α-LA in a pH range from 3 to 10 were analyzed. The degree of modification was higher than 40 %. The enzymatic lipophilization modified the functionality of the α-LA due to the increase in the surface hydrophobicity. In general, the surface properties were improved by the lipophilization specially at alkaline pH values, increasing the emulsifying activity more than 60 % and showing higher foam stability.

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KW - Functional properties

KW - Lipase

KW - Lipophilization

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Ffect of enzymatic lipophilization on the functional properties of bovine α-actalbumin

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