Factors affecting protein transfer into surfactant-isooctane solution: A case study of extraction behavior of chemically modified cytochrome c

Tsutomu Ono, Masahiro Goto

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The extraction mechanism of proteins by surfactant molecules in an organic solvent has been investigated using a chemically modified protein. We conducted guanidylation on lysine residues of cytochrome c by replacing their amino groups with homoarginine to enhance the protein-surfactant interaction. Results hate shown that guanidylated cytochrome c readily forms a hydrophobic complex with dioleyl phosphoric acid (DOLPA) through hydrogen bonding between the phosphate moiety and the guanidinium groups. Although improved protein-surfactant interaction activated the formation of a hydrophobic complex at the interface, it could not improve the protein transfer in isooctane. It has been established that the protein extraction mechanism using surfactant molecules is mainly governed by two processes: formation of an interfacial complex at the oil-water interface and the subsequent solubilization of the complex into the organic phase. In addition, a kinetic study demonstrated that guanidylation of lysine accelerated the initial extraction rate of cytochrome c. This fact implies that the protein transferability from aqueous phase into organic phase depends on the protein-surfactant interaction which can be modified by protein surface engineering.

Original languageEnglish
Pages (from-to)903-908
Number of pages6
JournalBiotechnology Progress
Volume14
Issue number6
DOIs
Publication statusPublished - Jan 1 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology

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