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Biospecific immobilization of mannan-penicillin G acylase neoglycoenzyme on Concanavalin A-bead cellulose

Mislovicova, D; Masarova, Jana LU ; Vikartovska, A; Gemeiner, P and Michalkova, E (2004) In Journal of Biotechnology 110(1). p.11-19
Abstract
The matter of this work was to evaluate possibilities of biospecific immobilization of synthetic mannan-penicillin G acylase neoglycoconjugate on Concanavalin A support. The conjugate containing 37% (w/w) of yeast mannan was prepared. Significant biospecific interaction of this neoglycoenzyme with Con A was confirmed by precipitation method. The biospecific sorption of conjugate was investigated using Concanavalin A-triazine bead celluloses MT-100 with different content of Con A (from 1.4 to 9.8 mg Con A/g wet support). The results obtained under optimal conditions were compared with those from covalent immobilization of PGA. The sorbent capacity was observed higher for covalent binding of enzyme. On the other hand, the biospecifically... (More)
The matter of this work was to evaluate possibilities of biospecific immobilization of synthetic mannan-penicillin G acylase neoglycoconjugate on Concanavalin A support. The conjugate containing 37% (w/w) of yeast mannan was prepared. Significant biospecific interaction of this neoglycoenzyme with Con A was confirmed by precipitation method. The biospecific sorption of conjugate was investigated using Concanavalin A-triazine bead celluloses MT-100 with different content of Con A (from 1.4 to 9.8 mg Con A/g wet support). The results obtained under optimal conditions were compared with those from covalent immobilization of PGA. The sorbent capacity was observed higher for covalent binding of enzyme. On the other hand, the biospecifically immobilized neoglycoenzyme retained a greater amount of initial activity. The maximum amount of 6.6 mg immobilized neoglycoenzyme/g wet Con A-sorbent (18.1 U/g) was achieved. The amount as well as activity of immobilized mannan-penicillin G acylase was increased by its two multiple layering on surface of sorbent (10.1 mg, respectively, 23.5 U/g wet sorbent). Determined storage and operational (using flow calorimetric method) stabilities of biospecifically immobilized enzyme, were similar, possibly somewhat higher that those of covalent bound penicillin G acylase. (C) 2004 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
enzyme stability, biospecific immobilization, Concanavalin A, neoglycoenzyme, penicillin G acylase, mannan from yeast
in
Journal of Biotechnology
volume
110
issue
1
pages
11 - 19
publisher
Elsevier
external identifiers
  • pmid:15099901
  • wos:000221492900002
  • scopus:1942535896
ISSN
1873-4863
DOI
10.1016/j.jbiotec.2004.01.006
language
English
LU publication?
yes
id
196fc3fc-e902-40a5-ba21-48be7af36e25 (old id 277909)
date added to LUP
2007-10-28 15:14:02
date last changed
2017-04-23 03:27:51
@article{196fc3fc-e902-40a5-ba21-48be7af36e25,
  abstract     = {The matter of this work was to evaluate possibilities of biospecific immobilization of synthetic mannan-penicillin G acylase neoglycoconjugate on Concanavalin A support. The conjugate containing 37% (w/w) of yeast mannan was prepared. Significant biospecific interaction of this neoglycoenzyme with Con A was confirmed by precipitation method. The biospecific sorption of conjugate was investigated using Concanavalin A-triazine bead celluloses MT-100 with different content of Con A (from 1.4 to 9.8 mg Con A/g wet support). The results obtained under optimal conditions were compared with those from covalent immobilization of PGA. The sorbent capacity was observed higher for covalent binding of enzyme. On the other hand, the biospecifically immobilized neoglycoenzyme retained a greater amount of initial activity. The maximum amount of 6.6 mg immobilized neoglycoenzyme/g wet Con A-sorbent (18.1 U/g) was achieved. The amount as well as activity of immobilized mannan-penicillin G acylase was increased by its two multiple layering on surface of sorbent (10.1 mg, respectively, 23.5 U/g wet sorbent). Determined storage and operational (using flow calorimetric method) stabilities of biospecifically immobilized enzyme, were similar, possibly somewhat higher that those of covalent bound penicillin G acylase. (C) 2004 Elsevier B.V. All rights reserved.},
  author       = {Mislovicova, D and Masarova, Jana and Vikartovska, A and Gemeiner, P and Michalkova, E},
  issn         = {1873-4863},
  keyword      = {enzyme stability,biospecific immobilization,Concanavalin A,neoglycoenzyme,penicillin G acylase,mannan from yeast},
  language     = {eng},
  number       = {1},
  pages        = {11--19},
  publisher    = {Elsevier},
  series       = {Journal of Biotechnology},
  title        = {Biospecific immobilization of mannan-penicillin G acylase neoglycoenzyme on Concanavalin A-bead cellulose},
  url          = {http://dx.doi.org/10.1016/j.jbiotec.2004.01.006},
  volume       = {110},
  year         = {2004},
}