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- Publisher
- Springer Journals
- Copyright
- Copyright © 2009 by Pleiades Publishing, Ltd.
- Subject
- Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
- ISSN
- 0003-6838
- eISSN
- 1608-3024
- DOI
- 10.1134/S0003683809050032
- Publisher site
- See Article on Publisher Site
Abstract
Alcaligenes faecalis penicillin G acylase has several desired features over other penicillin G acylases and its use in industry requires immobilization. In this work, two novel supports ZH-EP (epoxy type) and ZH-HA (epoxy-amino type) were used to immobilize Alcaligenes faecalis penicillin G acylase (AfPGA) with Eupergit C as reference. The saturation of immobilized protein on ZH-EP (269 mg/g, 116 h) and ZH-HA (296 mg/g, 15 h) was obtained more rapidly than Eupergit C (197 mg/g, 260 h). And the activity of immobilized AfPGA on ZH-EP (520 U/g) and ZH-HA (2200 U/g) was higher than that on Eupergit C (310 U/g). The properties of three immobilized enzymes were compared and no obvious difference was observed, which indicated that ZH-EP and ZH-HA were promised in industry.
Journal
Applied Biochemistry and Microbiology – Springer Journals
Published: Sep 13, 2009