Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures
The capacity of UV-C light to induce glycation and modify functional properties of systems containing freeze-dried egg white proteins and carbohydrates with increasing molecular weight (i.e., glucose, maltose, trehalose and maltodextrin) was studied. Color changes induced by light exposure were take...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/10/1/26 |
| _version_ | 1827699406557675520 |
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| author | Lara Manzocco Stella Plazzotta Sonia Calligaris |
| author_facet | Lara Manzocco Stella Plazzotta Sonia Calligaris |
| author_sort | Lara Manzocco |
| collection | DOAJ |
| description | The capacity of UV-C light to induce glycation and modify functional properties of systems containing freeze-dried egg white proteins and carbohydrates with increasing molecular weight (i.e., glucose, maltose, trehalose and maltodextrin) was studied. Color changes induced by light exposure were taken as typical indicators of glycation. Samples were then analyzed for selected physical (critical concentration, particle size and viscosity), chemical (ovalbumin content) and technofunctional properties (gelling temperature and foaming capacity). The presence of sugars during exposure to UV-C light promoted intense browning and decreased ovalbumin content by circa 30%. Concomitantly, up to a 3-fold increase in critical concentration of the aqueous suspensions of the irradiated protein-carbohydrate powders and changes in particle size were detected. These modifications were consistent with the development of non-enzymatic browning reactions upon UV-C light irradiation. Photoinduced glycation was associated to a decrease in viscosity, a tendency to form gel at temperature lower by up to 8 °C and a better capacity of foam stabilization. The intensity of these changes seems to be affected by the nature of the carbohydrates reacting with proteins, with longer carbohydrates able to produce systems with higher foam stability capacity. |
| first_indexed | 2024-03-10T13:49:21Z |
| format | Article |
| id | doaj.art-56c4c60327484acd8485b9030e073983 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T13:49:21Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-56c4c60327484acd8485b9030e0739832023-11-21T02:20:31ZengMDPI AGFoods2304-81582020-12-011012610.3390/foods10010026Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates MixturesLara Manzocco0Stella Plazzotta1Sonia Calligaris2Department of Agricultural, Food, Environmental and Animal Sciences, University of Udine, Via Sondrio 2/A, 33100 Udine, ItalyDepartment of Agricultural, Food, Environmental and Animal Sciences, University of Udine, Via Sondrio 2/A, 33100 Udine, ItalyDepartment of Agricultural, Food, Environmental and Animal Sciences, University of Udine, Via Sondrio 2/A, 33100 Udine, ItalyThe capacity of UV-C light to induce glycation and modify functional properties of systems containing freeze-dried egg white proteins and carbohydrates with increasing molecular weight (i.e., glucose, maltose, trehalose and maltodextrin) was studied. Color changes induced by light exposure were taken as typical indicators of glycation. Samples were then analyzed for selected physical (critical concentration, particle size and viscosity), chemical (ovalbumin content) and technofunctional properties (gelling temperature and foaming capacity). The presence of sugars during exposure to UV-C light promoted intense browning and decreased ovalbumin content by circa 30%. Concomitantly, up to a 3-fold increase in critical concentration of the aqueous suspensions of the irradiated protein-carbohydrate powders and changes in particle size were detected. These modifications were consistent with the development of non-enzymatic browning reactions upon UV-C light irradiation. Photoinduced glycation was associated to a decrease in viscosity, a tendency to form gel at temperature lower by up to 8 °C and a better capacity of foam stabilization. The intensity of these changes seems to be affected by the nature of the carbohydrates reacting with proteins, with longer carbohydrates able to produce systems with higher foam stability capacity.https://www.mdpi.com/2304-8158/10/1/26ultravioletUV-CMaillard reactionproteinsviscosityfoams |
| spellingShingle | Lara Manzocco Stella Plazzotta Sonia Calligaris Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures Foods ultraviolet UV-C Maillard reaction proteins viscosity foams |
| title | Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures |
| title_full | Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures |
| title_fullStr | Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures |
| title_full_unstemmed | Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures |
| title_short | Exploring the Potentialities of Photoinduced Glycation to Steer Protein Functionalities: The Study Case of Freeze-Dried Egg White Proteins/Carbohydrates Mixtures |
| title_sort | exploring the potentialities of photoinduced glycation to steer protein functionalities the study case of freeze dried egg white proteins carbohydrates mixtures |
| topic | ultraviolet UV-C Maillard reaction proteins viscosity foams |
| url | https://www.mdpi.com/2304-8158/10/1/26 |
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