Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis
Growing attempts are being made to rationally utilize foods for human health improvement and disease prevention. Milk proteins are well suited for this purpose, since they are widely consumed, offer nutritional benefits and have been shown to be potentially suitable carriers for bioactive ingredient...
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v38_n_p40_Perez http://hdl.handle.net/20.500.12110/paper_0268005X_v38_n_p40_Perez |
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paper:paper_0268005X_v38_n_p40_Perez2023-06-08T15:23:55Z Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis Pérez, Oscar E. β-lactoglobulin Folic acid Invitro digestion Nano-complexes Nano-particles Growing attempts are being made to rationally utilize foods for human health improvement and disease prevention. Milk proteins are well suited for this purpose, since they are widely consumed, offer nutritional benefits and have been shown to be potentially suitable carriers for bioactive ingredients, such as vitamins and nutraceuticals. This work characterizes the interactions between β-lactoglobulin (β-lg) and folic acid (FA) at different load ratio and their functional implications, in terms of colloidal behavior and digestibility. Dynamic light scattering, isothermal titration calorimetery and atomic force microscopy were used to investigate β-lg/FA nano-complexes (mean size<10nm) formed at protein:vitamin molar ratio 1:10, whereas three FA molecules were found to be bound to one protein molecule. Colloidal stability tests (3<pH<10) revealed that nano-complexes formation improved β-lg dissolution near its isoelectric point and at low pH-values. This was also found to be accompanied by a shift in zeta-potential values at pH=5 for pure β-lg (0.95±0.09mV) versus β-lg/FA nano-complexes (-20.13±1.29mV). SDS-PAGE analysis of digesta, collected from gastric and duodenal invitro digestion of β-lg and its nano-complexes, revealed no marked alterations in the proteolytic susceptibility of β-lg. The study findings show the interactions of FA and β-lg in the formation of nano-complexes may be harnessed for delivery of FA in clear beverages with minimal effects to the protein's sensitivity to proteolysis. © 2013 Elsevier Ltd. Fil:Pérez, O.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v38_n_p40_Perez http://hdl.handle.net/20.500.12110/paper_0268005X_v38_n_p40_Perez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
β-lactoglobulin Folic acid Invitro digestion Nano-complexes Nano-particles |
| spellingShingle |
β-lactoglobulin Folic acid Invitro digestion Nano-complexes Nano-particles Pérez, Oscar E. Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| topic_facet |
β-lactoglobulin Folic acid Invitro digestion Nano-complexes Nano-particles |
| description |
Growing attempts are being made to rationally utilize foods for human health improvement and disease prevention. Milk proteins are well suited for this purpose, since they are widely consumed, offer nutritional benefits and have been shown to be potentially suitable carriers for bioactive ingredients, such as vitamins and nutraceuticals. This work characterizes the interactions between β-lactoglobulin (β-lg) and folic acid (FA) at different load ratio and their functional implications, in terms of colloidal behavior and digestibility. Dynamic light scattering, isothermal titration calorimetery and atomic force microscopy were used to investigate β-lg/FA nano-complexes (mean size<10nm) formed at protein:vitamin molar ratio 1:10, whereas three FA molecules were found to be bound to one protein molecule. Colloidal stability tests (3<pH<10) revealed that nano-complexes formation improved β-lg dissolution near its isoelectric point and at low pH-values. This was also found to be accompanied by a shift in zeta-potential values at pH=5 for pure β-lg (0.95±0.09mV) versus β-lg/FA nano-complexes (-20.13±1.29mV). SDS-PAGE analysis of digesta, collected from gastric and duodenal invitro digestion of β-lg and its nano-complexes, revealed no marked alterations in the proteolytic susceptibility of β-lg. The study findings show the interactions of FA and β-lg in the formation of nano-complexes may be harnessed for delivery of FA in clear beverages with minimal effects to the protein's sensitivity to proteolysis. © 2013 Elsevier Ltd. |
| author |
Pérez, Oscar E. |
| author_facet |
Pérez, Oscar E. |
| author_sort |
Pérez, Oscar E. |
| title |
Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| title_short |
Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| title_full |
Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| title_fullStr |
Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| title_full_unstemmed |
Milk protein-vitamin interactions: Formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| title_sort |
milk protein-vitamin interactions: formation of beta-lactoglobulin/folic acid nano-complexes and their impactoninvitro gastro-duodenal proteolysis |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0268005X_v38_n_p40_Perez http://hdl.handle.net/20.500.12110/paper_0268005X_v38_n_p40_Perez |
| work_keys_str_mv |
AT perezoscare milkproteinvitamininteractionsformationofbetalactoglobulinfolicacidnanocomplexesandtheirimpactoninvitrogastroduodenalproteolysis |
| _version_ |
1768544775368081408 |