Immobilization of penicillin acylase from Escherichia coli on commercial sepabeads EC-EP carrier
نویسندگان
چکیده
منابع مشابه
IMMOBILIZATION OF PENICILLIN ACYLASE FROM Escherichia coli ON COMMERCIAL SEPABEADS EC-EP CARRIER
This paper reports the covalent immobilization of penicillin G acylase from E. coli on sepabeads EC-EP, an epoxy-activated polymethacrylic carrier, and describes kinetic properties of the immobilized enzyme. The selected enzyme belongs to a class of biocatalysts whose industrial interest is due to their versatility to mediate hydrolysis of penicillins and semi-synthetic β−lactam antibiotics syn...
متن کاملA new crystal form of penicillin acylase from Escherichia coli.
A new crystal form of penicillin acylase (penicillin amidohydrolase, E.C. 3.5.1.11) from Escherichia coli W (ATCC 11105) is reported. The crystals were grown using a combination of hanging-drop and streak-seeding methods. The crystals are in the monoclinic space group P2(1) with cell dimensions a = 51.52, b = 131.95, c = 64.43 A, beta = 106.12 degrees. There is one heterodimer in the asymmetric...
متن کاملImmobilization of penicillin G acylase using permeabilized Escherichia coli whole cells within chitosan beads
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...
متن کاملimmobilization of penicillin g acylase using permeabilized escherichia coli whole cells within chitosan beads
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...
متن کاملModulation of the microenvironment surrounding the active site of penicillin G acylase immobilized on acrylic carriers improves the enzymatic synthesis of cephalosporins.
The catalytic properties of penicillin G acylase (PGA) from Escherichia coli in kinetically controlled synthesis of β-lactam antibiotics are negatively affected upon immobilization on hydrophobic acrylic carriers. Two strategies have been here pursued to improve the synthetic performance of PGA immobilized on epoxy-activated acrylic carriers. First, an aldehyde-based spacer was inserted on the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Periodica Technologica
سال: 2007
ISSN: 1450-7188,2406-095X
DOI: 10.2298/apt0738173z