High pressure stability of protein complexes studied by static and dynamic light scattering |
| |
Authors: | Ronald Gebhardt Ulrich Kulozik |
| |
Institution: | 1. Chair for Food Process Engineering and Dairy Technology, Technische Universit?t München , Freising-Weihenstephan, Germany ronald.gebhardt@wzw.tum.de;3. Chair for Food Process Engineering and Dairy Technology, Technische Universit?t München , Freising-Weihenstephan, Germany;4. ZIEL Center of Nutrition and Food Research, Technology Section, Technische Universit?t München , Freising-Weihenstephan, Germany |
| |
Abstract: | The high pressure dissociation of hemocyanin prepared from the lobster Homarus americanus and casein micelles from cow milk were observed by in situ light scattering. The hemocyanin dodecamer dissociated via a hexamer into monomers in a two-step three-species reaction. The influence of ligands and the effector l-lactate on the dissociation behavior was investigated. While no effect by carbon monoxide after exchanging the ligand oxygen was observed, the addition of the effector l-lactate led to a decrease in the pressure stability. Due to a trimer intermediate which was found to be stabilized by l-lactate, the dissociation reaction in the presence of the effector was analyzed by a three-step four-species reaction. In the case of casein micelles, a two-step dissociation mechanism was found. The stabilizing interactions of casein micelles were identified and separated. |
| |
Keywords: | static and dynamic light scattering protein complexes ligand binding intermolecular interactions |
|
|