Potential applications of peroxidase from Luffa acutangula in biotransformation

Plant peroxidases are widely employed as biocatalysts in organic and inorganic compounds biotransformation. In the present study, a novel luffa peroxidase (LPrx) was extracted and purified to homogeneity from Luffa acutangula . The important physicochemical properties of an enzyme, such as optimum pH, temperature, molecular weight, pI, and amino acid sequences, were thoroughly investigated. The SDS-PAGE Gel electrophoresis and MALDI-TOF MS analysis were carried out to determine the molecular weight and the amino acid sequence of LPrx. The molecular weight of 37.7 kDa was obtained with a total of 332 amino acid sequences. The enzyme kinetics study was carried out using guaiacol as a substrate in the presence of H 2 O 2 . An inhibition study was carried out to explore the scope of LPrx in detecting heavy metal ions, such as Hg 2+ , Pd 2+ , Pb 2+ , Ln 2+ , and Ba 2+ . The catalytic actions of LPrx in the present study revealed that it could effectively catalyze the oxidation of phenols, aromatic amine and the halogenation of halides. This communication proposed possible routes for LPrx-mediated bioconversion of phenols and aromatic amine.