Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde

Shiwei Cheng; Dongzhi Wei; Qingxun Song; Xiangguo Zhao

doi:10.1007/s10529-006-9067-x

Immobilization of permeabilized whole cell penicillin G acylase from Alcaligenes faecalis using pore matrix crosslinked with glutaraldehyde

Biotechnol Lett. 2006 Jul;28(14):1129-33. doi: 10.1007/s10529-006-9067-x. Epub 2006 Jun 24.

Authors

Shiwei Cheng¹, Dongzhi Wei, Qingxun Song, Xiangguo Zhao

Affiliation

¹ State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai, PR China.

PMID: 16799762
DOI: 10.1007/s10529-006-9067-x

Abstract

The activity of penicillin G acylase from Alcaligenes faecalis increased 7.5-fold when cells were permeabilized with 0.3% (w/v) CTAB. The treated cells were entrapped by polyvinyl alcohol crosslinked with boric acid, and crosslinked with 2% (v/v) glutaraldehyde to increase the stability. The conversion yield of penicillin G to 6-aminopenicillanic acid was 75% by immobilized system in batch reaction. No activity was lost after 15 cycles and about 65% enzyme activity was retained at the end of the 31th cycle.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cell Culture Techniques / methods*
Cetrimonium
Cetrimonium Compounds / pharmacology*
Enzymes, Immobilized / chemistry
Enzymes, Immobilized / metabolism
Escherichia coli / drug effects
Escherichia coli / enzymology*
Glutaral / chemistry*
Penicillin Amidase / chemistry*
Penicillin Amidase / isolation & purification
Penicillin Amidase / metabolism*
Permeability
Porosity
Ultrafiltration / instrumentation
Ultrafiltration / methods*

Substances

Cetrimonium Compounds
Enzymes, Immobilized
Penicillin Amidase
Glutaral
Cetrimonium