Optimized polymer–enzyme electrostatic interactions significantly improve penicillin G amidase efficiency in charged PEGA polymers

Hydrolytic yields as high as 80% were obtained by using penicillin G amidase (PGA) on substrates anchored on optimized positively charged PEGA polymers. By increasing the amount of permanent charges inside the polymer, electrostatic interactions between the positively charged PEGA + and the negative...

Full description

Saved in:
Bibliographic Details
Published inTetrahedron Vol. 61; no. 4; pp. 971 - 976
Main Authors Basso, Alessandra, Maltman, Beatrice A., Flitsch, Sabine L., Margetts, Graham, Brazendale, Ian, Ebert, Cynthia, Linda, Paolo, Verdelli, Silvia, Gardossi, Lucia
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 24.01.2005
Subjects
Electrostatic interaction
Hydrolysis
PEGA polymers
Penicillin G amidase
Solid phase biocatalysis
Hydrolysis
Solid phase biocatalysis
PEGA polymers
Penicillin G amidase
Electrostatic interaction
Online AccessGet full text

Cover

More Information
Summary:Hydrolytic yields as high as 80% were obtained by using penicillin G amidase (PGA) on substrates anchored on optimized positively charged PEGA polymers. By increasing the amount of permanent charges inside the polymer, electrostatic interactions between the positively charged PEGA + and the negatively charged PGA (pI=5.2–5.4) were strengthened, thus favouring the accessibility of the bulky enzyme (MW=88 kDa) inside the pores. The effect of different amounts of charges on polymer swelling and protein retention inside the polymer was investigated and correlated to the enzyme efficiency demonstrating that electrostatic interactions predominate over swelling properties in determining enzyme accessibility. Graphical Abstract
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0040-4020
1464-5416
DOI:10.1016/j.tet.2004.11.015