Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/141018
- author
- Masarova, Jana LU ; Mislovicova, D ; Mendichi, R ; Svitel, Juraj LU ; Gemeiner, P and Danielsson, Bengt LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biotechnology and Applied Biochemistry
- volume
- 39
- issue
- 3
- pages
- 285 - 291
- publisher
- Wiley
- 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
- 2016-04-01 12:08:44
- date last changed
- 2022-01-26 23:25:18
@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 = {{Wiley}},
series = {{Biotechnology and Applied Biochemistry}},
title = {{Mannan-penicillin G acylase neoglycoproteins and their potential applications in biotechnology}},
url = {{http://www.babonline.org/bab/039/bab0390285.htm}},
volume = {{39}},
year = {{2004}},
}