5IO7

Bovine beta-lactoglobulin complex with dodecane at high pressure (0.43 GPa)

Summary for 5IO7

• Entry DOI: 10.2210/pdb5io7/pdb
• Related: 5IO5 5IO6
• Descriptor: Beta-lactoglobulin, DODECANE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: beta-lactoglobulin, lipocalin, transport protein
• Biological source: Bos taurus (Bovine)
• Cellular location: Secreted: P02754
• Total number of polymer chains: 1
• Total formula weight: 18506.96

Authors

Kurpiewska, K.,Biela, A. (deposition date: 2016-03-08, release date: 2016-03-16, Last modification date: 2024-10-23)

Primary citation

Kurpiewska, K.,Biela, A.,Loch, J.I.,Swiatek, S.,Jachimska, B.,Lewinski, K.
Investigation of high pressure effect on the structure and adsorption of beta-lactoglobulin.
Colloids Surf B Biointerfaces, 161:387-393, 2017

PubMed Abstract: β-Lactoglobulin, being one of the principal whey protein, is of huge importance to the food industry. Temperature/pressure effects on this small protein has been extensively studied by industry. To characterize biochemical properties of β-lactoglobulin after or during pressurization, a wide range of methods have been used thus far. In this study, for the first time, the pressure-induced conformation of β-lactoglobulin in the crystal state was determined, at pressure 430 MPa. Changes observed in the high pressure structure correlate with the physico-chemical properties of pressure-treated β-lactoglobulin obtained from dynamic light scattering, electrophoretic mobility and quartz crystal microbalance with dissipation monitoring measurements. A comparison between the β-lactoglobulin structures determined at both high and ambient pressure contrasts the stable nature of the protein core and adjacent loop fragments. At high pressure the β-lactoglobulin structure presents early signs of dimer dissociation, charge and conformational changes characteristic for initial unfolded intermediate as well as a significant modification of the binding pocket volume. Those observations are supported by changes in zeta potential values and results in increase affinity of the β-lactoglobulin adsorption onto gold surface. Observed pressure-induced structural modifications were previously suggested as an important factor contributing to β-lactoglobulin denaturation process. Presented studies provide detailed analysis of pressure-associated structural changes influencing β-lactoglobulin conformation and consequently its adsorption.

PubMed: 29112912
DOI: 10.1016/j.colsurfb.2017.10.069

Experimental method

X-RAY DIFFRACTION (2.85 Å)