Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study.

ABSTRACT:

Background

Laccases (EC 1.10.3.2) are multi-copper oxidoreductases with great biotechnological importance due to their high oxidative potential and utility for removing synthetic dyes, oxidizing phenolic compounds, and degrading pesticides, among others.

Methods

A real-time stability study (RTS) was conducted for a year, by using enzyme concentrates from 3 batches (L1, L3, and L4). For which, five temperatures 243.15, 277.15, 298.15, 303.15, 308.15, and 313.15 K were assayed. Using RTS data and the Arrhenius equation, we calculated the rPOXA 1B accelerated stability (AS). Molecular dynamics (MD) computational study results were very close to those obtained experimentally at four different temperatures 241, 278, 298, and 314 K.

Results

In the RTS, 101.16, 115.81, 75.23

SUBMITTER: Ardila-Leal LD 

PROVIDER: S-EPMC8178886 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature