Article ID Journal Published Year Pages File Type
70139 Journal of Molecular Catalysis B: Enzymatic 2012 7 Pages PDF
Abstract

Salt fractionated pointed gourd (Trichosanthes dioica) peroxidase–concanavalin A (PGP–Con A) complex expressed 79% of original peroxidase activity which decreased on entrapment into calcium alginate–pectin gel. Immobilized PGP–Con A complex retained 82.7% activity even at 60 °C which was achieved at pH 4.0. Urea treatment resulted in activity loss by ∼40%. With dioxane, immobilized PGP exhibited an activity of over 55% whereas an increasing concentration of dimethylformide resulted in decline. Activity of immobilized PGP–Con A was dependent on nature and concentration of detergent. Michaelis–Menten constant (Km) and Vmax for entrapped PGP–Con A complex was 0.08 mM and 15.7 mM/min, respectively.This study shows the efficacy, durability and sustainability of immobilized catalytic system which could be efficiently used for the removal of synthetic dyes from industrial effluents.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► PGP proteins were immobilized with Con A and entrapped on to calcium alginate pectin gel and assessed for catalytic activity. ► Peroxidase activity of soluble and immobilized PGP was examined under the influence of several denaturants. ► Km and Vmax for entrapped PGP–Con A complex was 0.083 mM and 15.7 mM/min, respectively. ► Immobilized PGP preparations could be exploited for developing bioreactors for the treatment of phenolic and organic pollutants.

Related Topics
Physical Sciences and Engineering Chemical Engineering Catalysis
Authors
, , , ,