Biospecific immobilization of mannan-penicillin G acylase neoglycoenzyme on Concanavalin A-bead cellulose
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/277909
- author
- Mislovicova, D ; Masarova, Jana LU ; Vikartovska, A ; Gemeiner, P and Michalkova, E
- organization
- publishing date
- 2004
- 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
- 2016-04-01 11:42:22
- date last changed
- 2022-02-18 03:40:17
@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}},
keywords = {{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}},
doi = {{10.1016/j.jbiotec.2004.01.006}},
volume = {{110}},
year = {{2004}},
}