Thermal aggregation of patatin studied in situ
article
In this work dynamic light scattering was used to study the thermal aggregation of patatin in situ, to elucidate the physical aggregation mechanism of the protein and to be able to relate the aggregation behavior to its structural properties. The dependence of the aggregation rates on the temperature and the ionic strength suggested a mechanism of slow coagulation, being both diffusion and chemically limited. The aggregation rate dependence on the protein concentration was in accordance with the mechanism proposed. The aggregation rates as obtained at temperatures ranging from 40 to 65 °C correlated well with unfolding of the protein at a secondary level. Small- angle neutron scattering and dynamic light scattering results were in good accordance; they revealed that native patatin has a cylindrical shape with a diameter and length of 5 and 9.8 nm, respectively.
Chemicals/CAS: Carboxylic Ester Hydrolases, EC 3.1.1.-; patatin protein, Solanum tuberosum; Plant Proteins
Chemicals/CAS: Carboxylic Ester Hydrolases, EC 3.1.1.-; patatin protein, Solanum tuberosum; Plant Proteins
Topics
TNO Identifier
235200
ISSN
00218561
Source
Journal of Agricultural and Food Chemistry, 47(11), pp. 4600-4605.
Pages
4600-4605
Files
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