Format:
1 Online-Ressource (ix, 106 Seiten)
,
Illustrationen, Diagramme
Content:
Proteins are amphiphilic and adsorb at liquid interfaces. Therefore, they can be efficient stabilizers of foams and emulsions. β-lactoglobulin (BLG) is one of the most widely studied proteins due to its major industrial applications, in particular in food technology. In the present work, the influence of different bulk concentration, solution pH and ionic strength on the dynamic and equilibrium pressures of BLG adsorbed layers at the solution/tetradecane (W/TD) interface has been investigated. Dynamic interfacial pressure (Π) and interfacial dilational elastic modulus (E’) of BLG solutions for various concentrations at three different pH values of 3, 5 and 7 at a fixed ionic strength of 10 mM and for a selected fixed concentration at three different ionic strengths of 1 mM, 10 mM and 100 mM are measured by Profile Analysis Tensiometer PAT-1 (SINTERFACE Technologies, Germany). A quantitative data analysis requires additional consideration of depletion due to BLG adsorption at the interface at low protein bulk concentrations. This fac…
Note:
Dissertation Universität Potsdam, Mathematisch-Naturwissenschaftliche Fakultät 2016
Additional Edition:
Erscheint auch als Druck-Ausgabe Won, Jooyoung Dynamic and equilibrium adsorption behaviour of [beta]-lactoglobulin at the solution/tetradecane interface Potsdam, 2016
Language:
English
Keywords:
Lactoglobulin
;
Grenzflächenspannung
;
Hochschulschrift
URN:
urn:nbn:de:kobv:517-opus4-99167
URL:
https://nbn-resolving.org/urn:nbn:de:kobv:517-opus4-99167
URL:
https://d-nb.info/1218792973/34