Effects of high hydrostatic pressure on the structure of bovine α-lactalbumin
2010
Rodiles-Lopez, J.O. | Arroyo-Maya, I.J. | Jaramillo-Flores, M.E. | Gutierrez-Lopez, G.F. | Hernandez-Arana, A. | Barbosa-Canovas, G.V. | Niranjan, K. | Hernandez-Sanchez, H.
The effects of high hydrostatic pressure (HHP) processing (at 200 to 600MPa, 25 to 55°C, and from 5 to 15min) on some structural properties of α-lactalbumin was studied in a pH range of 3.0 to 9.0. The range of HHP processes produced a variety of molten globules with differences in their surface hydrophobicity and secondary and tertiary structures. At pH values of 3 and 5, there was a decrease in the α-helix content concomitant with an increase in β-strand content as the pressure increased. No changes in molecular size due to HHP-induced aggregation were detected by sodium dodecyl sulfate-PAGE. All samples showed higher thermostability as the severity of the treatment increased, indicating the formation of a less labile structure related to the HHP treatment.
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