On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers

Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under cond...

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Autores principales: Zema, P., Pilosof, A.M.R.
Formato: JOUR
Materias:
Aggregation
Delivery
Folic acid
Gelatin
pH
β-lactoglobulin
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0268005X_v79_n_p509_Zema
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_0268005X_v79_n_p509_Zema
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spelling todo:paper_0268005X_v79_n_p509_Zema2023-10-03T15:13:52Z On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers Zema, P. Pilosof, A.M.R. Aggregation Delivery Folic acid Gelatin pH β-lactoglobulin Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3). © 2018 Elsevier Ltd JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0268005X_v79_n_p509_Zema
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Aggregation
Delivery
Folic acid
Gelatin
pH
β-lactoglobulin
spellingShingle Aggregation
Delivery
Folic acid
Gelatin
pH
β-lactoglobulin
Zema, P.
Pilosof, A.M.R.
On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
topic_facet Aggregation
Delivery
Folic acid
Gelatin
pH
β-lactoglobulin
description Folic acid (FA) encapsulation in protein matrices has been reported as a suitable method for preventing FA degradation upon storage or processing as well as to improve its bioavailability. The ability of β-lactoglobulin (β-lg) and type A gelatin (G) to bind FA and form nano/microparticles under conditions of concentration (up to 5% w/w) and pH (3–7) that could have a technological application has been studied. The degree of folic acid binding to the proteins depended on their pH-dependent ζ-potential, indicating the occurrence of ionic bonds. Regardless of FA concentration, the percentage of bound FA to β-lg or G was 100% at pH 3. At pH 3, the size of particles strongly increased by increasing the molar FA/protein ratio. Protein aggregation and further flocculation was observed at higher molar ratios. However, the size of particles could be modulated by high intensity ultrasound application. FA/protein particles formed at pH 3 were totally reversible by shifting back the pH to 7. This pH dependence is strongly favorable for the delivery of FA at the duodene (pH 7) and for the protection of FA at the pH prevailing in the stomach (pH 3). © 2018 Elsevier Ltd
format JOUR
author Zema, P.
Pilosof, A.M.R.
author_facet Zema, P.
Pilosof, A.M.R.
author_sort Zema, P.
title On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_short On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_full On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_fullStr On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_full_unstemmed On the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
title_sort on the binding of folic acid to food proteins performing as vitamin micro/nanocarriers
url http://hdl.handle.net/20.500.12110/paper_0268005X_v79_n_p509_Zema
work_keys_str_mv AT zemap onthebindingoffolicacidtofoodproteinsperformingasvitaminmicronanocarriers
AT pilosofamr onthebindingoffolicacidtofoodproteinsperformingasvitaminmicronanocarriers
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