Water has also an important role in protein unfolding,
proteins being very pressure stable in the dry state (Smeller,
2002). Dumay, Picart, Regnault, and Thiebaud (2006) also
proposed that cold protein denaturation under pressure
could be reversible, reducing aggregation after pressure
release. This could be related to the reversible myoglobin
unfolding suggested for our frozen + pressurised samples,
where lower protein aggregation would take place in frozen
state due to the minimised molecular transport, not only
due to the low-temperature but also to the reduced free
water population. Finally, it must be remembered that
the observed reduction in a values could also be caused
by an increase in light reflection originated by the aggregation
of other proteins without actual alteration of
myoglobin.
Water has also an important role in protein unfolding,proteins being very pressure stable in the dry state (Smeller,2002). Dumay, Picart, Regnault, and Thiebaud (2006) alsoproposed that cold protein denaturation under pressurecould be reversible, reducing aggregation after pressurerelease. This could be related to the reversible myoglobinunfolding suggested for our frozen + pressurised samples,where lower protein aggregation would take place in frozenstate due to the minimised molecular transport, not onlydue to the low-temperature but also to the reduced freewater population. Finally, it must be remembered thatthe observed reduction in a values could also be causedby an increase in light reflection originated by the aggregationof other proteins without actual alteration ofmyoglobin.
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