The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes
In this study, the interaction of native and transglutaminase (Tgase) cross-linked β-lactoglobulin (β-LG) with caffeic acid (CA) was examined, aiming to obtain functional composites. Knowledge on the binding affinity and interaction mechanism was provided by performing fluorescence spectroscopy meas...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-07-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/10/8/1096 |
| _version_ | 1827712415456821248 |
|---|---|
| author | Nicoleta Stănciuc Gabriela Râpeanu Gabriela Elena Bahrim Iuliana Aprodu |
| author_facet | Nicoleta Stănciuc Gabriela Râpeanu Gabriela Elena Bahrim Iuliana Aprodu |
| author_sort | Nicoleta Stănciuc |
| collection | DOAJ |
| description | In this study, the interaction of native and transglutaminase (Tgase) cross-linked β-lactoglobulin (β-LG) with caffeic acid (CA) was examined, aiming to obtain functional composites. Knowledge on the binding affinity and interaction mechanism was provided by performing fluorescence spectroscopy measurements, after heating the native and cross-linked protein at temperatures ranging from 25 to 95 °C. Regardless of the protein aggregation state, a static quenching mechanism of intrinsic fluorescence of β-LG by CA was established. The decrease of the Stern–Volmer constants with the temperature increase indicating the facile dissociation of the weakly bound complexes. The thermodynamic analysis suggested the existence of multiple contact types, such as Van der Waals’ force and hydrogen bonds, between β-LG and CA. Further molecular docking tests indicated the existence of various CA binding sites on the β-LG surface heat-treated at different temperatures. Anyway, regardless of the simulated temperature, the CA-β-LG assemblies appeared to be unstable. Compared to native protein, the CA-β-LG and CA-β-LG<sub>Tgase</sub> complexes (ratio 1:1) exhibited significantly higher antioxidant activity and inhibitory effects on α-glucosidase, α-amylase, and pancreatic lipase, enzymes associated with metabolic syndrome. These findings might help the knowledge-based development of novel food ingredients with valuable biological properties. |
| first_indexed | 2024-03-10T18:14:36Z |
| format | Article |
| id | doaj.art-0585b566e747429a88e7d1a093c43edf |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T18:14:36Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-0585b566e747429a88e7d1a093c43edf2023-11-20T07:45:07ZengMDPI AGBiomolecules2218-273X2020-07-01108109610.3390/biom10081096The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional ComplexesNicoleta Stănciuc0Gabriela Râpeanu1Gabriela Elena Bahrim2Iuliana Aprodu3Faculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domnească Street, 800201 Galați, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domnească Street, 800201 Galați, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domnească Street, 800201 Galați, RomaniaFaculty of Food Science and Engineering, Dunarea de Jos University of Galati, 111 Domnească Street, 800201 Galați, RomaniaIn this study, the interaction of native and transglutaminase (Tgase) cross-linked β-lactoglobulin (β-LG) with caffeic acid (CA) was examined, aiming to obtain functional composites. Knowledge on the binding affinity and interaction mechanism was provided by performing fluorescence spectroscopy measurements, after heating the native and cross-linked protein at temperatures ranging from 25 to 95 °C. Regardless of the protein aggregation state, a static quenching mechanism of intrinsic fluorescence of β-LG by CA was established. The decrease of the Stern–Volmer constants with the temperature increase indicating the facile dissociation of the weakly bound complexes. The thermodynamic analysis suggested the existence of multiple contact types, such as Van der Waals’ force and hydrogen bonds, between β-LG and CA. Further molecular docking tests indicated the existence of various CA binding sites on the β-LG surface heat-treated at different temperatures. Anyway, regardless of the simulated temperature, the CA-β-LG assemblies appeared to be unstable. Compared to native protein, the CA-β-LG and CA-β-LG<sub>Tgase</sub> complexes (ratio 1:1) exhibited significantly higher antioxidant activity and inhibitory effects on α-glucosidase, α-amylase, and pancreatic lipase, enzymes associated with metabolic syndrome. These findings might help the knowledge-based development of novel food ingredients with valuable biological properties.https://www.mdpi.com/2218-273X/10/8/1096caffeic acidβ-lactoglobulincomplexationantioxidantantidiabeticbinding |
| spellingShingle | Nicoleta Stănciuc Gabriela Râpeanu Gabriela Elena Bahrim Iuliana Aprodu The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes Biomolecules caffeic acid β-lactoglobulin complexation antioxidant antidiabetic binding |
| title | The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes |
| title_full | The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes |
| title_fullStr | The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes |
| title_full_unstemmed | The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes |
| title_short | The Interaction of Bovine β-Lactoglobulin with Caffeic Acid: From Binding Mechanisms to Functional Complexes |
| title_sort | interaction of bovine β lactoglobulin with caffeic acid from binding mechanisms to functional complexes |
| topic | caffeic acid β-lactoglobulin complexation antioxidant antidiabetic binding |
| url | https://www.mdpi.com/2218-273X/10/8/1096 |
| work_keys_str_mv | AT nicoletastanciuc theinteractionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT gabrielarapeanu theinteractionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT gabrielaelenabahrim theinteractionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT iulianaaprodu theinteractionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT nicoletastanciuc interactionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT gabrielarapeanu interactionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT gabrielaelenabahrim interactionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes AT iulianaaprodu interactionofbovineblactoglobulinwithcaffeicacidfrombindingmechanismstofunctionalcomplexes |