Kinetics of Formation and Functional Properties of Conjugates Prepared by Dry-State Incubation of β-Lactoglobulin/Acacia Gum Electrostatic Complexes

The formation of conjugates between β-lactoglobulin and acacia gum based on electrostatic complexes formed at pH 4.2 was investigated upon dry-state incubation for up to 14 days at 60 °C and 79% relative humidity (RH). By means of SEC-HPLC and RP-HPLC, it was shown that the β-lactoglobulin incubated...

Full description

Saved in:
Bibliographic Details
Published inJournal of agricultural and food chemistry Vol. 53; no. 23; pp. 9089 - 9099
Main Authors Schmitt, Christophe, Bovay, Claudine, Frossard, Philippe
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 16.11.2005
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:The formation of conjugates between β-lactoglobulin and acacia gum based on electrostatic complexes formed at pH 4.2 was investigated upon dry-state incubation for up to 14 days at 60 °C and 79% relative humidity (RH). By means of SEC-HPLC and RP-HPLC, it was shown that the β-lactoglobulin incubated alone was able to form polymers with molecular masses higher than 200 kDa until 50% of the initial monomeric protein disappeared after 14 days. In the presence of acacia gum at initial protein to polysaccharide weight mixing ratios of 2:1 and 1:2, only 35% of the initial β-lactoglobulin monomers disappeared after 14 days. Using RP-HPLC, an apparent reaction order of 2 was found for the disappearance of monomeric β-lactoglobulin both in the presence or absence of acacia gum. However, the reaction rate was faster in the absence of acacia gum. SDS−PAGE electrophoresis with silver staining confirmed the formation of β-lactoglobulin/acacia gum conjugates. The solubility curves of the incubated β-lactoglobulin showed a minimum around pH 4−5. By contrast, the minimum of solubility of the β-lactoglobulin/acacia gum incubated mixtures shifted to lower pH values compared to initial mixtures. The conjugates exhibited higher foam capacity than the incubated protein as well as lower equilibrium air/water surface tension. Conjugation at ratio 1:2 led to increased interfacial viscosity (300 mN s m-1 at 0.01 Hz) compared to β-lactoglobulin alone (100 mN s m-1 at 0.01 Hz), but similar interfacial elasticity (30−40 mN m-1). The foam capacity of the conjugates was significantly higher than that of the incubated β-lactoglobulin as well as foam expansion and drainage time, especially at pH 5.3, i.e., higher than the pH of formation of the conjugates. Keywords: Dry-state incubation; reaction kinetics; protein polymerization; solubility; interfacial properties; foaming properties
Bibliography:istex:AC07AE69651EBDD277C6C4632F267F456BD148CC
ark:/67375/TPS-H0RGPWDH-8
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-8561
1520-5118
DOI:10.1021/jf051630t