AMBIENTUM BIOETHICA BIOLOGIA CHEMIA DIGITALIA DRAMATICA EDUCATIO ARTIS GYMNAST. ENGINEERING EPHEMERIDES EUROPAEA GEOGRAPHIA GEOLOGIA HISTORIA HISTORIA ARTIUM INFORMATICA IURISPRUDENTIA MATHEMATICA MUSICA NEGOTIA OECONOMICA PHILOLOGIA PHILOSOPHIA PHYSICA POLITICA PSYCHOLOGIA-PAEDAGOGIA SOCIOLOGIA THEOLOGIA CATHOLICA THEOLOGIA CATHOLICA LATIN THEOLOGIA GR.-CATH. VARAD THEOLOGIA ORTHODOXA THEOLOGIA REF. TRANSYLVAN
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Autori: ANDREA VARGA, ZSÓFIA BATA, PÁL CSUKA, DIANA MONICA BORDEA, BEÁTA G. VÉRTESSY, ADRIANA MARCOVICI, FLORIN DAN IRIMIE, LÁSZLÓ POPPE, LÁSZLÓ CSABA BENCZE.
DOI: https://doi.org/10.24193/subbchem.2017.3.25
Published Online: 2017-09-30
Published Print: 2017-09-30
VIEW PDF: A NOVEL PHENYLALANINE…
This study describes the cloning of the gene encoding a novel phenylalanine ammonia-lyase from Kangiella koreensis (KkPAL) into pET19b expression vector. Optimization of protein expression and purification conditions yielded 15 mg pure soluble protein from one liter of E. coli culture. Enzymatic activity measurements of the ammonia elimination reaction from different natural aromatic amino acids proved the protein to be a phenylalanine ammonia-lyase. The isolated protein showed remarkably high, 81.7 °C melting temperature, making it especially suitable for biocatalytic applications.
Keywords: phenylalanine ammonia-lyase, Kangiella koreensis, protein expression, optimization
