Projekt per år
Sammanfattning
Copper radical alcohol oxidases belonging to auxiliary activity family 5, subfamily 2 (AA5_2) catalyze the oxidation of galactose and galactosides, as well as aliphatic alcohols. Despite their broad applied potential, so far very few AA5_2 members have been biochemically characterized. We report the recombinant production and biochemical characterization of an AA5_2 oxidase from Penicillium rubens Wisconsin 54-1255 (PruAA5_2A), which groups within an unmapped clade phylogenetically distant from those comprising AA5_2 members characterized to date. PruAA5_2 preferentially oxidized raffinose over galactose; however, its catalytic efficiency was 6.5 times higher on glycolaldehyde dimer compared to raffinose. Deep sequence analysis of characterized AA5_2 members highlighted amino acid pairs correlated to substrate range and conserved within the family. Moreover, PruAA5_2 activity spans substrate preferences previously reported for AA5 subfamily 1 and 2 members, identifying possible functional overlap across the AA5 family.
Originalspråk | engelska |
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Artikelnummer | 0216546 |
Tidskrift | PLoS One |
Volym | 14 |
Nummer | 5 |
Sidor (från-till) | 1-19 |
Antal sidor | 19 |
ISSN | 1932-6203 |
DOI | |
Status | Publicerad - 15 maj 2019 |
MoE-publikationstyp | A1 Tidskriftsartikel-refererad |
Vetenskapsgrenar
- 414 Jordbruksbioteknologi
- 1183 Växtbiologi, mikrobiologi, virologi
Projekt
- 1 Slutfört
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Novel selective carbohydrate oxidizing enzymes for targeted polymer and fiber modification (ENOX)
Parikka, K. (Deltagare), Juvonen, M. (Deltagare), Koutaniemi, S. (Deltagare) & Tenkanen, M. (Annan)
01/09/2011 → 31/08/2014
Projekt: Forskningsprojekt