Foam fractionation is a simple, inexpensive method for separating and purif
ying proteins. Typically, a dilute bromelain solution with a pH ranging fro
m 2.0 to 7.0 foams very well when bubbles are introduced into a foam fracti
onation column. It was observed, however, that the dilute enzyme solution o
nly foamed between approximately pH 2.0 and 3.0 when the inner wall of the
fractionation column was coated with a natural contaminant (okra residue).
We studied the separation ratio and the protein mass recovery to explore th
e effect of a natural antifoaming agent on the foam fractionation of a dilu
te bromelain solution. The control variables used in this process were the
initial bulk solution pH, which ranged from 2.0 to 7.0, and the superficial
air velocity, which varied between 1.7 and 6.2 cm/s.