Purification and characterisation of new laccase from Trametes polyzona WRF03.

ABSTRACT: The molecular screening for laccase specific gene sequences in Trametes polyzona WRF03 (TpWRF03) using designed oligonucleotide primers analogous to the conserved sequences on the copper-binding regions of known laccases showed positive amplification with an amplicon size corresponding to 1500 bp. The purified TpWRF03 laccase (TpL) is a monomer with a molecular weight corresponding to 66?kDa. The enzyme had an optimal pH of 4.5 and temperature of 55?°C. TpL was most stable within pH of 5.5-6.5 and at a temperature range of 40-50?°C. Sodium azide, sodium cyanide and Fe²⁺ greatly inhibited the enzyme activity. TpL showed more than 50 % decolourisation efficiency on coomassie brilliant blue (72.35 %) and malachite green (57.84 %) but displayed low decolourisation efficiency towards Azure B (1.78 %) and methylene blue (0.38 %). The results showed that TpWRF03 produces high-yield of true laccase with robust properties for biotechnological applications.

SUBMITTER: Ezike TC 

PROVIDER: S-EPMC7701954 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature