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Peroxidase-active cell free extract from onion solid wastes: biocatalytic properties and putative pathway of ferulic acid oxidation

Paper ID Volume ID Publish Year Pages File Format Full-Text
22300 43267 2008 7 PDF Available
Title
Peroxidase-active cell free extract from onion solid wastes: biocatalytic properties and putative pathway of ferulic acid oxidation
Abstract

The exploitation of food residuals can be a major contribution in reducing the polluting load of food industry waste and in developing novel added-value products. Plant food residues including trimmings and peels might contain a range of enzymes capable of transforming bioorganic molecules, and thus they may have potential uses in several biocatalytic processes, including green organic synthesis, modification of food physicochemical properties, bioremediation, etc. Although the use of bacterial and fungal enzymes has gained attention in studies pertaining to biocatalytic applications, plant enzymes have been given less consideration or even disregarded. Therefore, we investigated the use of a crude peroxidase preparation from solid onion by-products for oxidizing ferulic acid, a widespread phenolic acid, various derivatives of which may occur in food wastes. The highest enzyme activity was observed at a pH value of 4, but considerable activity was retained up to a pH value of 6. Favorable temperatures for increased activity varied between 20–40°C, 30°C being the optimal. Liquid chromatography-mass spectrometry analysis of a homogenate/H2O2-treated ferulic acid solution showed the formation of a dimer as a major oxidation product.

Keywords
biocatalysis; bioremediation; ferulic acid; onion; peroxidase4-AAP, 4-aminoantipyrine; BGP, bitter gourd peroxidase; CA, caffeic acid; CouA, p-coumaric acid; DAD, diode array detector; DMF, dimethyl formamide; ESI, electrospray ionisation; FA, ferulic aci
First Page Preview
Peroxidase-active cell free extract from onion solid wastes: biocatalytic properties and putative pathway of ferulic acid oxidation
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 106, Issue 3, September 2008, Pages 279–285
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering