TY - JOUR
T1 - Effects of high hydrostatic pressure on the structure of bovine α-lactalbumin
AU - Rodiles-López, J. O.
AU - Arroyo-Maya, I. J.
AU - Jaramillo-Flores, M. E.
AU - Gutiérrez-López, G. F.
AU - Hernández-Arana, A.
AU - Barbosa-Cánovas, G. V.
AU - Niranjan, K.
AU - Hernández-Sánchez, H.
N1 - Funding Information:
This work was partially financed by the Instituto Politécnico Nacional (Mexico City, Mexico). Octavio Rodiles-López and Izlia J. Maya Arroyo thank the Consejo Nacional de Ciencia y Tecnología (Mexico City, Mexico) for the awarding of their scholarship. Authors Jaramillo-Flores, Gutiérrez-López, and Hernández-Sánchez also acknowledge the fellowship from COFAA-IPN (Mexico City, Mexico).
PY - 2010/4
Y1 - 2010/4
N2 - The effects of high hydrostatic pressure (HHP) processing (at 200 to 600 MPa, 25 to 55°C, and from 5 to 15 min) 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.
AB - The effects of high hydrostatic pressure (HHP) processing (at 200 to 600 MPa, 25 to 55°C, and from 5 to 15 min) 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.
KW - High hydrostatic pressure
KW - Molecular property
KW - Protein structure
KW - α-lactalbumin
UR - http://www.scopus.com/inward/record.url?scp=77949944071&partnerID=8YFLogxK
U2 - 10.3168/jds.2009-2786
DO - 10.3168/jds.2009-2786
M3 - Artículo
C2 - 20338419
SN - 0022-0302
VL - 93
SP - 1420
EP - 1428
JO - Journal of Dairy Science
JF - Journal of Dairy Science
IS - 4
ER -