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Continuous foaming for protein recovery: Part I. Recovery of β‐casein
Author(s) -
Brown A. K.,
Kaul A.,
Varley J.
Publication year - 1999
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19990205)62:3<278::aid-bit4>3.0.co;2-d
Subject(s) - chromatography , chemistry , casein , absorbance , circular dichroism , volumetric flow rate , fluorescence spectroscopy , factorial experiment , polyacrylamide gel electrophoresis , analytical chemistry (journal) , polyacrylamide , fluorescence , biochemistry , physics , statistics , mathematics , quantum mechanics , polymer chemistry , enzyme
Foam separation is known to have potential for separation of biological molecules with a range of surface activities. A statistical study (factorial design) was carried out to establish the optimum operating conditions for the continuous foam separation of β‐casein. Maximum values of enrichment of β‐casein into the foam phase were found for low levels of initial feed protein concentration, gas flow rate, feed‐flow rate, and high foam heights. Maximum values of protein recovery, were generally found at high levels of initial feed protein concentration, gas‐flow rate, feed‐flow rate, and low foam heights. The highest values obtained for enrichment and separation ratio were 54.7 and 181.3, respectively, with a simultaneous protein recovery of 62%; thus, illustrating the potential effectiveness of this technique. The effect of foaming on protein conformation is also important, and in this study protein structure was analyzed before and after foam separation experiments. Techniques used were: native polyacrylamide gel electrophoresis (PAGE), UV absorbance spectroscopy, circular dichroism, and fluorescence. Native PAGE showed no detectable changes in protein structure. However, absorbance scanning, fluorimetry, and circular dichroism revealed some conformational changes over a range of concentration effects. © 1999 John Wiley & Sons, Inc. Biotechnol Bioeng 62: 278–290, 1999.