Probing the interaction of catechin and its β-CD inclusion complex with different food models. (February 2019)
- Record Type:
- Journal Article
- Title:
- Probing the interaction of catechin and its β-CD inclusion complex with different food models. (February 2019)
- Main Title:
- Probing the interaction of catechin and its β-CD inclusion complex with different food models
- Authors:
- Ho, Siyin
Thoo, Yin Yin
Young, David James
Siow, Lee Fong - Abstract:
- Abstract: We have previously reported that the antioxidant activity of catechin degraded dramatically in a protein rich matrix compared to a sugar or oil-based matrix, and that this degradation was significantly retarded by β-cyclodextrin (β-CD) encapsulation. In the present study, we have probed the nature of this interaction of catechin and its β-CD inclusion complex with protein, sugar and oil models using fourier-transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. The former technique revealed a shift and increase in the intensity of the protein amide absorption bands upon mixing with catechin that was not observed with β-CD or with the corresponding encapsulated catechin, suggesting hydrogen bonding between this antioxidant and the protein amide groups. Catechin fluorescence was quenched by all three food models in a concentration dependent manner and this relationship was used to calculate binding constants in each matrix, which also revealed a strong interaction between catechin and protein that was reduced by encapsulation with β-CD. These new results help to explain our earlier observation of catechin degradation by protein and have implications for the use of this important antioxidant in food formulations. Highlights: Free catechin degraded dramatically in protein compared to a sugar and oil model. Strong interaction was observed between catechin and protein. Weak interaction was observed between β-CD encapsulated catechin and protein. β-CDAbstract: We have previously reported that the antioxidant activity of catechin degraded dramatically in a protein rich matrix compared to a sugar or oil-based matrix, and that this degradation was significantly retarded by β-cyclodextrin (β-CD) encapsulation. In the present study, we have probed the nature of this interaction of catechin and its β-CD inclusion complex with protein, sugar and oil models using fourier-transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. The former technique revealed a shift and increase in the intensity of the protein amide absorption bands upon mixing with catechin that was not observed with β-CD or with the corresponding encapsulated catechin, suggesting hydrogen bonding between this antioxidant and the protein amide groups. Catechin fluorescence was quenched by all three food models in a concentration dependent manner and this relationship was used to calculate binding constants in each matrix, which also revealed a strong interaction between catechin and protein that was reduced by encapsulation with β-CD. These new results help to explain our earlier observation of catechin degradation by protein and have implications for the use of this important antioxidant in food formulations. Highlights: Free catechin degraded dramatically in protein compared to a sugar and oil model. Strong interaction was observed between catechin and protein. Weak interaction was observed between β-CD encapsulated catechin and protein. β-CD encapsulation helps to protect catechin from degradation. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 100(2019)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 100(2019)
- Issue Display:
- Volume 100, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 100
- Issue:
- 2019
- Issue Sort Value:
- 2019-0100-2019-0000
- Page Start:
- 368
- Page End:
- 373
- Publication Date:
- 2019-02
- Subjects:
- Cyclodextrin -- Inclusion complex -- Encapsulation -- Functional foods -- Protein models
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2018.10.069 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23783.xml