Abstract:
:Relatively conservative modifications of three proteins were carried out to alter their surface properties. The protein properties modified were hydrophobicity and charge. This was done by acylation of amino groups with anhydrides. For the hydrophobic modification experiments, two proteins (beta-lactoglobulin and bovine serum albumin [BSA]) and four anhydrides (hexanoic, butyric, succinic, acetic) were used. For the modification of surface charge the protein thaumatin was selected and various proportions of the free amino groups were blocked with acetic anhydride to give a series of proteins with differing isoelectric points. Detailed characterization and purification of selected modified proteins was carried out including molecular weight measurements and conformational analysis. The criteria used for selecting the modified proteins for subsequent investigation of their partitioning in aqueous two-phase systems (ATPS) is described. With a judicious choice of starting material it was found that limited chemical modifications to proteins could effectively alter surface hydrophobicity or charge almost independently, with little effect on other molecular properties. It appears, however, that the method for chemical modification and the reaction conditions must also be carefully controlled. (c) 1996 John Wiley & Sons, Inc.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Franco TT,Andrews AT,Asenjo JAdoi
10.1002/(SICI)1097-0290(19960205)49:3<290::AID-BITsubject
Has Abstractpub_date
1996-02-05 00:00:00pages
290-9issue
3eissn
0006-3592issn
1097-0290journal_volume
49pub_type
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