title: Kinetic modeling of the thermal aggregation of patatin.
abstract: A kinetic model of the thermal aggregation of patatin is presented based on chromatographic analysis of the proportions of nonaggregated and aggregated patatin. It was observed that the decrease of the amount of nonaggregated patatin proceeded initially quickly and was followed by slower aggregation at longer incubation times. It was shown that this behavior was not due to heterogeneity of the starting material. It was noted that overestimation of the amount of native molecules after a heat treatment, caused by refolding of the unfolded protein during the cooling step prior to the analysis, was significant and could not be neglected. Hence, corrections based on information on the structural properties of patatin were applied. Taking this into account, a model was proposed consisting of a first-order formation of reactive particles, followed by a second-order aggregation reaction. This model described the thermal aggregation of patatin rather accurately and was confirmed by experiments at various protein concentrations.
authors.affiliation: Centre for Protein Technology TNO-WAU, Wageningen, The Netherlands.
authors.forename: A M
authors.initials: AM
authors.lastname: Pots
authors.forename: H
authors.initials: H
authors.lastname: Gruppen
authors.forename: H H
authors.initials: HH
authors.lastname: de Jongh
authors.forename: M A
authors.initials: MA
authors.lastname: van Boekel
authors.forename: P
authors.initials: P
authors.lastname: Walstra
authors.forename: A G
authors.initials: AG
authors.lastname: Voragen
mesh_terms: D002265:Carboxylic Ester Hydrolases; D002850:Chromatography, Gel; D007700:Kinetics; D008956:Models, Chemical; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013696:Temperature
chemical_list: D010940:Plant Proteins; C043222:patatin protein, Solanum tuberosum; D002265:Carboxylic Ester Hydrolases