Abstract
ABSTRACTConformational changes in bovine serum albumin (BSA), Ca++‐free α‐lactalbumin(apo‐α‐lac), and Ca++‐saturated α‐lactalbumin(holo‐ct‐lac) were examined via Fourier transform infrared (FTIR) spectroscopy after pressure treatment up to 1270 MPa. BSA showed minimal irreversible secondary structural changes with pressurization, showing a slight loss of β‐sheet structure in favor of α‐helix. Apo‐α‐lac underwent major irreversible changes and exhibited infrared bands characteristic of aggregation upon decompression. Holo‐α‐lac showed extensive resistance to high pressure with no major structural changes. The rich disulfide content in BSA and the presence of Ca++ in holo‐α‐lac may play important roles in stabilizing these proteins against pressure denaturation.
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