Catalytic and antimicrobial properties of α-amylase immobilised on the surface of metal oxide nanoparticles
Authors:
- Olga Długosz,
- Julia Matysik,
- Wiktoria Matyjasik,
- Marcin Banach
Abstract
New methods of obtaining products containing enzymes reduce the costs associated with obtaining them, increase the efficiency of processes and stabilize the created biocatalytic systems. In the study a catalytic system containing the enzyme a-amylase immobilized on ZnO nanoparticle and Fe3O4 nanoparticles was created. The efficiency of the processes was obtained with variables: concentrations of enzymes, temperatures and times, to define the best conditions for running the process, for which were determined equilibrium and kinetics of adsorption. The most effective parameters of a-amylase immobilization on metal oxides were determined, obtaining 100.8 mg/g sorption capacity for ZnO and 102.9 mg/g for Fe3O4 nanoparticles. Base on the best parameters, ZnO-a-amylase was investigated as an antimicrobial agent and Fe3O4-aamylase was tested as a catalyst in the process of starch hydrolysis. As a result of the conducted experiments, it was found that a-amylase immobilized on Fe3O4 nanoparticles maintained high catalytic activity (the reaction rate constant KM= 0.7799 [g/dm3 ] and the maximum reaction rate Vmax = 8.660 [g/(dm3 min)]).
- Record ID
- CUT2cfed85e869440a4b3811117d26219b8
- Publication categories
- ;
- Author
- Journal series
- Journal of Cluster Science, ISSN 1040-7278, e-ISSN 1572-8862
- Issue year
- 2021
- Vol
- 32
- No
- 6
- Pages
- 1609-1622
- Other elements of collation
- fot.; schem.; tab.; wykr.; Bibliografia (na s.) - 1621-1622; Bibliografia (liczba pozycji) - 39; Oznaczenie streszczenia - Abstr.; Data udostępnienia on-line - 2020-11-01; Numeracja w czasopiśmie - Vol. 32, Iss. 6
- Keywords in English
- α-amylase, metal oxide nanoparticles, immobilization, nanobiocatalytic material
- DOI
- DOI:10.1007/s10876-020-01921-5 Opening in a new tab
- URL
- https://link.springer.com/article/10.1007/s10876-020-01921-5 Opening in a new tab
- Language
- eng (en) English
- License
- Score (nominal)
- 70
- Publication indicators
- Citation count
- 15
- Additional fields
- Indeksowana w: Web of Science, Scopus
- Uniform Resource Identifier
- https://cris.pk.edu.pl/info/article/CUT2cfed85e869440a4b3811117d26219b8/
- URN
urn:pkr-prod:CUT2cfed85e869440a4b3811117d26219b8
* presented citation count is obtained through Internet information analysis, and it is close to the number calculated by the Publish or PerishOpening in a new tab system.