SURFACTANT MODIFIED ENZYMES - SOLUBILITY AND ACTIVITY OF SURFACTANT-MODIFIED CATALASE IN ORGANIC-SOLVENTS

Authors
JENE Q PEARSON JC LOWE CR
Citation
Q. Jene et al., SURFACTANT MODIFIED ENZYMES - SOLUBILITY AND ACTIVITY OF SURFACTANT-MODIFIED CATALASE IN ORGANIC-SOLVENTS, Enzyme and microbial technology, 20(1), 1997, pp. 69-74
Citations number
26
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Enzyme and microbial technology → ACNP
ISSN journal
01410229
Volume
20
Issue
1
Year of publication
1997
Pages
69 - 74
Database
ISI
SICI code
0141-0229(1997)20:1<69:SME-SA>2.0.ZU;2-W
Abstract
Catalase could be dissolved in a range of organic solvents by modifyin g less than 5% of its surface amino groups with a reactive nonionic su rfactant derivative, bis(brij35). A solution of brij35-modified catala se in I,I,1-trichloroethylene displayed substantially greater activity than PEG modified enzyme. Modification of the enzyme surface with bri j35 may facilitate enzyme solution through the formation of small enzy me aggregates enclosed within a reverse micelle formed from free and c ovalently bound brij35. (C) 1997 by Elsevier Science Inc.