Genetic Modification of the Penicillin G Acylase Surface To Improve Its Reversible Immobilization on Ionic Exchangers
نویسندگان
چکیده
منابع مشابه
Genetic modification of the penicillin G acylase surface to improve its reversible immobilization on ionic exchangers.
A new mutant of the industrial enzyme penicillin G acylase (PGA) from Escherichia coli has been designed to improve its reversible immobilization on anionic exchangers (DEAE- or polyethyleneimine [PEI]-coated agarose) by assembling eight new glutamic residues distributed homogeneously through the enzyme surface via site-directed mutagenesis. The mutant PGA is produced and processed in vivo as i...
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The objective of this work was to study enzyme immobilization on chitosan activated with glutaraldehyde, aiming to produce a cheap biocatalyst. Two different immobilization strategies were studied: one-point and multipoint covalent attachment to the solid matrix. The multipoint covalent attachment derivative had an 82% immobilization yield. It was 4.9-fold more stable than the free enzyme at 50...
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The PGA enzyme belongs to the family of N-terminal nucleophile (Ntn) hydrolases. The enzyme Penicillin G Acylase (PGA) mainly produced from Penicillium chrysogenum, E.coli. The synthesis of PGA enzyme is depends on the physico-chemical parameters like carbon source, pH, temperature and media were optimized for higher production of enzyme. There are different methods of purification of PGA enzym...
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The different ionic molecules/compounds were used as a ligand for the immobilization of penicillin G acylase on the highly porous cellulose-based polymeric membrane having buffer flux 1,746 LMH (L m(-2) h(-1)) at 0.5 bar pressure. The immobilized enzyme activity around 250 U(App) was obtained with the ligand such as proline, tryptophan, casein acid hydrolysate, and brilliant green. Comparativel...
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Entrapment of permeabilized whole cells within a matrix is a common method for immobilization. Chitosan possesses distinct chemical and biological properties, which make it a suitable matrix for entrapment and immobilization of penicillin G acylase (PGA). In the first step, Escherichia coli (ATCC 11105) cells were permeabilized using N-cetyl-N,N,N-trimethyl ammonium bromide (CTAB) (0.1% w/v, 45...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2007
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.02107-06