title: Comparison of heat-induced aggregation of globular proteins.
abstract: Typically, heat-induced aggregation of proteins is studied using a single protein under various conditions (e.g., temperature). Because different studies use different conditions and methods, a mechanistic relationship between molecular properties and the aggregation behavior of proteins has not been identified. Therefore, this study investigates the kinetics of heat-induced aggregation and the size/density of formed aggregates for three different proteins (ovalbumin, β-lactoglobulin, and patatin) under various conditions (pH, ionic strength, concentration, and temperature). The aggregation rate of β-lactoglobulin was slower (>10 times) than that of ovalbumin and patatin. Moreover, the conditions (pH, ionic strength, and concentration) affected the aggregation kinetics of β-lactoglobulin more strongly than for ovalbumin and patatin. In contrast to the kinetics, for all proteins the aggregate size/density increased with decreasing electrostatic repulsion. By comparing these proteins under these conditions, it became clear that the aggregation behavior cannot easily be correlated to the molecular properties (e.g., charge and exposed hydrophobicity).
authors.affiliation: †Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
authors.forename: Roy J B M
authors.initials: RJ
authors.lastname: Delahaije
authors.affiliation: †Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
authors.forename: Peter A
authors.initials: PA
authors.lastname: Wierenga
authors.affiliation: §AVEBE, Prins Hendrikplein 20, 9641 GK Veendam, The Netherlands.
authors.forename: Marco L F
authors.initials: ML
authors.lastname: Giuseppin
authors.affiliation: †Laboratory of Food Chemistry, Wageningen University, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
authors.forename: Harry
authors.initials: H
authors.lastname: Gruppen
mesh_terms: D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D007782:Lactoglobulins / Q000737:chemistry*; D009994:Osmolar Concentration; D010047:Ovalbumin / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D066329:Protein Aggregates; D055672:Static Electricity
chemical_list: D007782:Lactoglobulins; D010940:Plant Proteins; D066329:Protein Aggregates; C043222:patatin protein, Solanum tuberosum; D010047:Ovalbumin; D002265:Carboxylic Ester Hydrolases
keywords: concentration; ionic strength; ovalbumin; pH; patatin; β-lactoglobulin