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The effects of pH and ionic strength on the partitioning of four proteins in reverse micelle systems

1994; Wiley; Volume: 43; Issue: 11 Linguagem: Inglês

10.1002/bit.260431108

1097-0290

Bárbara A. Andrews, D.L. Pyle, Juan A. Asenjo,

Chemical and Physical Properties in Aqueous Solutions

Abstract Four proteins with different physicochemical properties have been partitioned in reversed micelle systems: thaumatin, ribonuclease A, soybean trypsin inhibitor, and α‐lactalbumin. The organic phase was formed by sodium salt (AOT) in isooctane, and the aqueous phase contained KCl, KBr, MgCl 2 , or NaCl. Aqueous phase pH was varied between 2 and 13 and ionic strength from 0.1 to 1.0 M . Small changes in pH [around the isoelecric point (pl)] were found to influence the solubilization of ribonuclease A and trypsin inhibitor, but for thaumatin the pH change necessary to affect partition was much greater as a consequence of the difference in net charge (titration curves) of these protein molecules as pH changes. The type of ions present in the system was also a determining factor for partition; the larger ions (K + ) produced more electrostatic screening and hence less protein solubilization than the smaller ions (Na + ). With changes in ionic strength surface hydrophobicity was a dominant factor affecting solubilization of thaumatin in NaCl‐containing systems at high pH. Charge distribution and hydrophobicity are thought to be important parameters when partitioning the protein α‐lactalbumin. © 1994 John Wiley & Sons, Inc.