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Quantitative Immunofluorescence to Measure Global Localized Translation
Published on: August 22, 2017
Nisin quantification by ELISA allows the modeling of its apparent diffusion coefficient in model cheeses
Samar Aly1, Juliane Floury, Marie-Hélène Famelart
1INRA, UMR1253, Science and Technology of Milk and Eggs, F-35000 Rennes, France.
Journal of Agricultural and Food Chemistry
|July 21, 2011
Summary
This study measured peptide diffusion in model cheeses, finding that adding gelatin significantly slowed nisin diffusion. These findings highlight how cheese composition impacts solute movement during ripening.
Area of Science:
- Food Science
- Biochemistry
- Chemical Engineering
Background:
- Solute diffusion is crucial for enzymatic reactions during cheese ripening.
- Limited data exists on peptide diffusion in cheese compared to salt.
- Nisin, a bacteriocin peptide, plays a role in cheese properties.
Purpose of the Study:
- To quantify the apparent diffusion coefficients of nisin in model cheeses.
- To investigate the effect of cheese composition (gelatin addition) on peptide diffusion.
- To establish a foundation for understanding peptide transport in cheese.
Main Methods:
- Utilized a profile concentration device for nisin migration studies.
- Employed a specifically developed enzyme-linked immunosorbent assay (ELISA) for nisin quantification.
- Modeled apparent diffusion coefficients using Fick's law.
Main Results:
- The average apparent diffusion coefficient for nisin in ultrafiltered (UF) cheese was 49.5 μm²/s.
- Adding 10% gelatin to the UF retentate reduced the nisin diffusion coefficient to 34.4 μm²/s.
- Differences in cheese macrostructure and microstructure correlated with diffusion rates.
Conclusions:
- This study presents the first apparent diffusion coefficients for a peptide in cheese.
- Cheese composition and microstructure significantly influence the diffusion of small solutes like peptides.
- Findings support the hypothesis that structural properties affect peptide mobility in cheese.
