Data di Pubblicazione:
2000
Citazione:
Thermal stabilities of lupin seed conglutin γ protomers and tetramers / M. Duranti, F. Sessa, A. Scarafoni, T. Bellini, F. Dallocchio. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 1520-5118. - 48:4(2000), pp. 1118-1123. [10.1021/jf9907384]
Abstract:
Various experimental approaches have been used in this work to assess the thermal stabilities of lupin seed conglutin γ at two pH values, 4.5 and 7.5, at which the protein exists as a protomer and a tetramer, respectively. The patterns of thermal unfolding at the two pH values differed significantly; the tetramer aggregated and became insoluble, whereas the protomer was still soluble after thermal treatment. Also, the midpoint transition temperatures were dramatically different, being 60.3 and 75.1 °C for the protomer and tetramer, respectively. The behavior of conglutin γ at neutral pH was also affected by disulfide formation/interchange, in that some unfolded protein molecules became covalently stabilized. More detailed analyses by differential scanning calorimetry and indirect fluorescence measurements, using 8-anilino-1-naphthalenesulfonic acid as a probe, confirmed the remarkable differences observed in the thermal stabilities of the two protein forms and allowed models for their unfolding patterns to be drawn.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Conglutin γ; Lupinus albus; Oligomeric protein; Thermal stability
Elenco autori:
M. Duranti, F. Sessa, A. Scarafoni, T. Bellini, F. Dallocchio
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