Stabilization of penicillin G acylase by immobilization on glutaraldehyde-activated chitosan
نویسندگان
چکیده
منابع مشابه
Stabilization of Penicillin G Acylase by Immobilization on Glutaraldehyde-activated Chitosan
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...
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 کاملGenetic 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...
متن کاملImmobilization of keratinolytic metalloprotease from Chryseobacterium sp. strain kr6 on glutaraldehyde-activated chitosan.
Keratinases are exciting keratin-degrading enzymes; however, there have been relatively few studies on their immobilization. A keratinolytic protease from Chryseobacterium sp. kr6 was purified and its partial sequence determined using mass spectrometry. No significant homology to other microbial peptides in the NCBI database was observed. Certain parameters for immobilization of the purified ke...
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: Brazilian Journal of Chemical Engineering
سال: 2005
ISSN: 0104-6632
DOI: 10.1590/s0104-66322005000400005