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Interactions and diffusion in fine-stranded beta-lactoglobulin gels determined via FRAP and binding
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
RISE, SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, SIK – Institutet för livsmedel och bioteknik.
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2014 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 106, no 1, p. 253-262Article in journal (Refereed) Published
Abstract [en]

The effects of electrostatic interactions and obstruction by the microstructure on probe diffusion were determined in positively charged hydrogels. Probe diffusion in fine-stranded gels and solutions of ?-lactoglobulin at pH 3.5 was determined using fluorescence recovery after photobleaching (FRAP) and binding, which is widely used in biophysics. The microstructures of the ?-lactoglobulin gels were characterized using transmission electron microscopy. The effects of probe size and charge (negatively charged Na2-fluorescein (376Da) and weakly anionic 70kDa FITC-dextran), probe concentration (50 to 200 ppm), and ?-lactoglobulin concentration (9% to 12% w/w) on the diffusion properties and the electrostatic interaction between the negatively charged probes and the positively charged gels or solutions were evaluated. The results show that the diffusion of negatively charged Na2-fluorescein is strongly influenced by electrostatic interactions in the positively charged ?-lactoglobulin systems. A linear relationship between the pseudo-on binding rate constant and the ?-lactoglobulin concentration for three different probe concentrations was found. This validates an important assumption of existing biophysical FRAP and binding models, namely that the pseudo-on binding rate constant equals the product of the molecular binding rate constant and the concentration of the free binding sites. Indicators were established to clarify whether FRAP data should be analyzed using a binding-diffusion model or an obstruction-diffusion model. © 2014 by the Biophysical Society.

Place, publisher, year, edition, pages
2014. Vol. 106, no 1, p. 253-262
Keywords [en]
Food Engineering
Keywords [sv]
Livsmedelsteknik
National Category
Food Science
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URN: urn:nbn:se:ri:diva-8400DOI: 10.1016/j.bpj.2013.11.2959PubMedID: 24411257OAI: oai:DiVA.org:ri-8400DiVA, id: diva2:966271
Available from: 2016-09-08 Created: 2016-09-08 Last updated: 2018-08-15Bibliographically approved

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Loren, Niklas

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