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Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology

Masarova, Jana LU ; Mislovicova, D; Mendichi, R; Svitel, Juraj LU ; Gemeiner, P and Danielsson, Bengt LU (2004) In Biotechnology and Applied Biochemistry 39(3). p.285-291
Abstract
Mannan-penicillin G acylase neoglycoproteins were prepared by the conjugation of Saccharomyces cerevisiae mannan with enzyme penicillin G acylase using the reductive amination method. Eight neoglycoproteins preparations were obtained after gel chromatography. The preparations contained from 42 to 67% (w/w) saccharides and their molar masses varied from 283 to over 1000 kDa. Significant biospecific interaction of separated fractions with the lectin concanavalin A was evaluated by the precipitation and sorption method (equilibrium constants) and further characterized using surface plasmon resonance to determine kinetic association and dissociation constants. K-D was determined over the range 10(-7) M. High-molar-mass preparations appeared to... (More)
Mannan-penicillin G acylase neoglycoproteins were prepared by the conjugation of Saccharomyces cerevisiae mannan with enzyme penicillin G acylase using the reductive amination method. Eight neoglycoproteins preparations were obtained after gel chromatography. The preparations contained from 42 to 67% (w/w) saccharides and their molar masses varied from 283 to over 1000 kDa. Significant biospecific interaction of separated fractions with the lectin concanavalin A was evaluated by the precipitation and sorption method (equilibrium constants) and further characterized using surface plasmon resonance to determine kinetic association and dissociation constants. K-D was determined over the range 10(-7) M. High-molar-mass preparations appeared to be more suitable for preparation of stable and active complexes with concanavalin A for prospective use as a penicillin G acylase biocatalyst in enzyme reactors. The enzyme stability of such complexes was significantly increased compared with the original neoglycoprotein. Lower-molar-mass preparations were more suitable for applications such as biocatalysts in bioanalytical devices. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biotechnology and Applied Biochemistry
volume
39
issue
3
pages
285 - 291
publisher
Portland Press
external identifiers
  • wos:000222039500004
  • scopus:2942701993
ISSN
1470-8744
language
English
LU publication?
yes
id
94e491f7-ff0b-4fa0-9a9d-d496f7a44b15 (old id 141018)
alternative location
http://www.babonline.org/bab/039/bab0390285.htm
date added to LUP
2007-07-16 10:38:24
date last changed
2017-01-01 04:52:53
@article{94e491f7-ff0b-4fa0-9a9d-d496f7a44b15,
  abstract     = {Mannan-penicillin G acylase neoglycoproteins were prepared by the conjugation of Saccharomyces cerevisiae mannan with enzyme penicillin G acylase using the reductive amination method. Eight neoglycoproteins preparations were obtained after gel chromatography. The preparations contained from 42 to 67% (w/w) saccharides and their molar masses varied from 283 to over 1000 kDa. Significant biospecific interaction of separated fractions with the lectin concanavalin A was evaluated by the precipitation and sorption method (equilibrium constants) and further characterized using surface plasmon resonance to determine kinetic association and dissociation constants. K-D was determined over the range 10(-7) M. High-molar-mass preparations appeared to be more suitable for preparation of stable and active complexes with concanavalin A for prospective use as a penicillin G acylase biocatalyst in enzyme reactors. The enzyme stability of such complexes was significantly increased compared with the original neoglycoprotein. Lower-molar-mass preparations were more suitable for applications such as biocatalysts in bioanalytical devices.},
  author       = {Masarova, Jana and Mislovicova, D and Mendichi, R and Svitel, Juraj and Gemeiner, P and Danielsson, Bengt},
  issn         = {1470-8744},
  language     = {eng},
  number       = {3},
  pages        = {285--291},
  publisher    = {Portland Press},
  series       = {Biotechnology and Applied Biochemistry},
  title        = {Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology},
  volume       = {39},
  year         = {2004},
}