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...
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Published in | Journal of agricultural and food chemistry Vol. 53; no. 23; pp. 9089 - 9099 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
16.11.2005
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Subjects | |
Online Access | Get full text |
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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 |
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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 |