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A novel peroxidase from runner bean ( Phaseolus coccineus L.): Enhanced affinity purification, characterization, and dye decolorization activity
Author(s) -
Oztekin Aykut,
Tasbasi Seyma
Publication year - 2020
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/jfbc.13411
Subject(s) - peroxidase , chemistry , yield (engineering) , enzyme , chromatography , substrate (aquarium) , ionic strength , enzyme assay , redox , specific activity , phaseolus , size exclusion chromatography , nuclear chemistry , biochemistry , organic chemistry , aqueous solution , materials science , botany , biology , ecology , metallurgy
In this study, a novel runner bean peroxidase (RBP) was purified and characterized. Affinity‐based purification was performed with newly synthesized disubstituted 4‐aminobenzohydrazides. In the purification results, 253‐fold was achieved with a yield of 56.2%. Furthermore, molecular weight and enzyme purity were checked with the SDS‐PAGE and observed a single band at 31.2 kDa. Optimum conditions were determined as temperature = 50°C, ionic strength = 0.2 M, and pH 7.0. Enzyme exhibited 31.2% of residual activity in the presence of 20% DMSO. Additionally, the redox‐mediated decolorization effect of the enzyme was examined for Reactive Blue 19 and Acid Blue 25 dyes. As a result of 1‐hr incubation, the enzyme removal activity of Reactive Blue 19 and Acid Blue 25 dyes was calculated as 47% and 57%, respectively. Practical applications Peroxidases (PODs) ability to catalyze various redox reactions for many substrates makes them significant enzymes in industrial sectors. In our current report, a single‐step strategy was developed and followed as an alternative to multi‐step methods commonly used for the purification of PODs. During this process, high yield was achieved and the separation time was shortened. Also, the purification of RBP that can potentially supplant PODs used in the industrial applications was carried out for the first time. In addition, substrate specificity, catalytic behavior in water‐miscible organic solvents, and dye bleaching activity of this enzyme have been determined to evaluate the utilization capacity in various processes.

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