Cell wall bound anionic peroxidases from asparagus byproducts

J Agric Food Chem. 2014 Oct 8;62(40):9644-50. doi: 10.1021/jf502560k. Epub 2014 Sep 22.

Abstract

Asparagus byproducts are a good source of cationic soluble peroxidases (CAP) useful for the bioremediation of phenol-contaminated wastewaters. In this study, cell wall bound peroxidases (POD) from the same byproducts have been purified and characterized. The covalent forms of POD represent >90% of the total cell wall bound POD. Isoelectric focusing showed that whereas the covalent fraction is constituted primarily by anionic isoenzymes, the ionic fraction is a mixture of anionic, neutral, and cationic isoenzymes. Covalently bound peroxidases were purified by means of ion exchange chromatography and affinity chromatography. In vitro detoxification studies showed that although CAP are more effective for the removal of 4-CP and 2,4-DCP, anionic asparagus peroxidase (AAP) is a better option for the removal of hydroxytyrosol (HT), the main phenol present in olive mill wastewaters.

Keywords: anionic isoperoxidase; asparagus byproduct; bioremediation; cell wall bound peroxidase; phenols.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Asparagus Plant / enzymology*
  • Biodegradation, Environmental
  • Cell Wall / metabolism*
  • Chlorophenols / isolation & purification
  • Chromatography, Ion Exchange
  • Enzyme Stability
  • Hydrogen-Ion Concentration
  • Industrial Waste
  • Isoelectric Focusing
  • Kinetics
  • Peroxidases / chemistry*
  • Peroxidases / isolation & purification*
  • Peroxidases / metabolism
  • Phenylethyl Alcohol / analogs & derivatives
  • Phenylethyl Alcohol / isolation & purification
  • Wastewater / chemistry*

Substances

  • Chlorophenols
  • Industrial Waste
  • Waste Water
  • sulfonated 2,4-dichlorophenol
  • 3,4-dihydroxyphenylethanol
  • 4-chlorophenol
  • Peroxidases
  • anionic peroxidase
  • Phenylethyl Alcohol