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                                       Details van artikel 34 van 39 gevonden artikelen
 
 
  THE KINETICS OF THE REACTIONS CATALYZED BY AN ENZYMATIC PREPARATION PRODUCED BY A BACILLUS LICHENIFORMIS STRAIN
 
 
Titel: THE KINETICS OF THE REACTIONS CATALYZED BY AN ENZYMATIC PREPARATION PRODUCED BY A BACILLUS LICHENIFORMIS STRAIN
Auteur: DRAGOMIRESCU MONICA
VINTILĒ T.
VLAD-OROS BEATRICE
PREDA GABRIELA
Verschenen in: Lucrari stiintifice. Zootehnie si biotehnologii
Paginering: Jaargang 40 (2007) nr. 1 pagina's 85-90
Jaar: 2007
Inhoud: Robust immobilization techniques that preserve the activity of biomolecules havemany potential applications. In recent years, a number of new bioimobilisationmethods in sol-gel-derived materials were reported. The interactions between thebiomolecule and the inorganic material determine the degree to which thebiomolecule retains its native properties. The newer technological developments inthe field of immobilized biocatalysts can offer the possibility of a wider and moreeconomical exploitation of biocatalysts in biological applications, food and feedindustry, medicine, and in the development of bioprocess monitoring devices, like thebiosensors.The aim of this study was to obtain immobilized enzymatic preparations by methodswhich affect enzyme conformations and kinetic parameters as less as possible. Weimmobilized the enzymatic preparation with protease activity produced by a Bacilluslicheniformis B 40 local strain by physical bonding on ceramics and entrapment intosol-gel-derived glasses obtained from tetraethyl orthosilicate (TEOS), deposited inthin layer on a ceramic support (entrapment/deposition). Both physically adsorbedand entrapped/deposited enzymes follow Michaelis-Menten kinetics, similar with thesoluble enzyme. In the case of immobilized enzymes, the apparent Michaelisconstant, Km, was greater than that of the native one, as it was expected. The kineticparameters indicate that the enzymatic preparations adsorbed on ceramic supportand entrapped/deposited show less affinity for the substrate, Km being 1.3 and 2.1times higher than that of the native enzyme, respectively. The maximum velocityincreased also by 3.5 and 7.9 times respectively, compared with the free counterpart(according to Lineweaver-Burk linearization).
Uitgever: Facultatea de Zootehnie si Biotehnologii, Timisoara (provided by DOAJ)
Bronbestand: Elektronische Wetenschappelijke Tijdschriften
 
 

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