1999
DOI: 10.1021/jf980886e
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Heat-Induced Aggregation of β-Lactoglobulin as a Function of pH

Abstract: The effect of pH in the range 6.0-8.0 on the denaturation and aggregation of beta-lactoglobulin (beta-lg) was investigated. Results were interpreted in terms of the reaction scheme for the denaturation and aggregation of beta-lg proposed by Roefs and De Kruif (Eur. J. Biochem. 1994, 226, 883-889). The rate of conversion of native beta-lg increased strongly at higher pH values, whereas the molecular mass of the aggregates decreased strongly. In the pH range 6.4-8.0 aggregates were formed mainly by intermolecula… Show more

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Cited by 154 publications
(147 citation statements)
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“…The increase of temperature causes a reversible unfolding of the monomer followed by an irreversible aggregation. Association between these aggregates forms larger aggregates with different characteristics depending on the heat treatment and pH values (HOFFMANN & VAN MIL, 1999). The increased size of aggregates induces the increased particles volume fraction resulting in a more viscous solution (VARDHANABHUTI & FOEGEDING, 1999).…”
Section: Resultsmentioning
confidence: 99%
“…The increase of temperature causes a reversible unfolding of the monomer followed by an irreversible aggregation. Association between these aggregates forms larger aggregates with different characteristics depending on the heat treatment and pH values (HOFFMANN & VAN MIL, 1999). The increased size of aggregates induces the increased particles volume fraction resulting in a more viscous solution (VARDHANABHUTI & FOEGEDING, 1999).…”
Section: Resultsmentioning
confidence: 99%
“…As a result, the conversion of thiols into disulphide bonds increased with pH up to at least 6.9 [163] or up to pH 11 [113], as did the contribution of intermolecular disulphide bonds in the formation of heatinduced protein aggregates of β-lactoglobulin [67] or of κ-casein and whey protein in milk [57]. Conversely, the contribution of electrostatic interactions decreased as pH increased, as a result of the increased negative charge of the β-lactoglobulin (isoelectric pH ~ 5.4) [67].…”
Section: Disulphide Bonds Number and Size Of The Heat-induced Proteimentioning
confidence: 95%
“…The disulfide bridges are known to be a key factor that affects the gel strength (Hoffmann and Van Mil, 1999;Creamer et al, 2004) and the aggregation process through the polymerization of monomers to form large polymer chains. However, there is only limited availability of the bonds to be formed and hence excessively longer heating time may not be effective anymore.…”
Section: Effect Of Heating Time On Hiwpg Dissolutionmentioning
confidence: 99%