IMMOBILIZATION OF PHENYLALANINE AMMONIA-LYASE ON HYDROXYAPATITE AND HYDROXYAPATITE COMPOSITES

Judith-Hajnal BARTHA-VARI; Renáta ELEKES-DARABONT; Laura-Edit BARABÁS; Réka BARABÁS

doi:10.24193/subbchem.2021.1.13

IMMOBILIZATION OF PHENYLALANINE AMMONIA-LYASE ON HYDROXYAPATITE AND HYDROXYAPATITE COMPOSITES

Authors

Judith-Hajnal BARTHA-VARI Babeş-Bolyai University, Faculty of Chemistry and Chemical Engineering, 11 Arany Janos str., RO-400028, Cluj-Napoca, Romania. https://orcid.org/0000-0001-7147-9651
Renáta ELEKES-DARABONT Babeş-Bolyai University, Faculty of Chemistry and Chemical Engineering, 11 Arany Janos str., RO-400028, Cluj-Napoca, Romania.
Laura-Edit BARABÁS Babeş-Bolyai University, Faculty of Chemistry and Chemical Engineering, 11 Arany Janos str., RO-400028, Cluj-Napoca, Romania.
Réka BARABÁS Babeş-Bolyai University, Faculty of Chemistry and Chemical Engineering, 11 Arany Janos str., RO-400028, Cluj-Napoca, Romania. *Corresponding author: breka@chem.ubbcluj.ro https://orcid.org/0000-0001-6730-084X

DOI:

https://doi.org/10.24193/subbchem.2021.1.13

Keywords:

hydroxyapatite, composites, carbon nanotubes, gelatin, chitosan, phenylalanine ammonia-lyase, immobilization, ammonia elimination.

Abstract

A new and efficient immobilization method of phenylalanine ammonia-lyase was obtained using hydroxyapatite (HAP) and hydroxyapatite - carbon nanotube, gelatin and chitosan - composites (HAP-CNT, HAP-GEL and HAP-CS) as support material. HAP and HAP composites were characterized by transmission electron microscopy (TEM), laser diffraction particle size analyzer and XRD measurements. The obtained nanobioconjugates were tested in the ammonia elimination reactions from L-phenylalanine (L-1). The reusability and the time-course profile of the immobilized enzyme preparation was also tested. While the biocatalyst obtained by using HAP-CS-15 as support material provided the highest conversion rate in the ammonia elimination reaction from L-1 (98,1% compared to 98,5% obtained using the non-immobilized enzyme), the most stable biocatalyst proved to be HAP-PAL, which maintained more than 80% of its initial activity even after 5 cycles of reuse.

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STUDIA UBB CHEMIA, Volume 66 (LXVI), No. 1, March 2021

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Published

2021-03-30

How to Cite

BARTHA-VARI, J.-H., ELEKES-DARABONT, R., BARABÁS, L.-E., & BARABÁS, R. (2021). IMMOBILIZATION OF PHENYLALANINE AMMONIA-LYASE ON HYDROXYAPATITE AND HYDROXYAPATITE COMPOSITES. Studia Universitatis Babeș-Bolyai Chemia, 66(1), 165–178. https://doi.org/10.24193/subbchem.2021.1.13