Purification and characterisation of a polyphenol oxidase from Boletus erythropus and investigation of its catalytic efficiency in selected organic solvents


FOOD CHEMISTRY, vol.119, no.3, pp.1044-1049, 2010 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 119 Issue: 3
  • Publication Date: 2010
  • Doi Number: 10.1016/j.foodchem.2009.08.011
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1044-1049
  • Recep Tayyip Erdoğan University Affiliated: Yes


Polyphenol oxidase (PPO) was purified from Boletus erythropus using a Sepharose 4B-L-tyrosine-p-amino benzoic acid affinity column. Optimum pH and temperature were found to be 8.0 and 20 degrees C, respectively, using 4-methylcatechol as a substrate. The enzyme was extremely stable between pH 3.0 and 9.0 after 24 h incubation at 4 degrees C. B. erythropus PPO was also quite stable between 10 and 30 degrees C after 4 h incubation. The K-m and V-max values were calculated as 2.8 mM and 1430 U/mg protein by Lineweaver-Burk curve, respectively. The enzyme activity was inhibited by sodium metabisulfite, ascorbic acid, sodium azide and benzoic acid. It was seen that the mushroom PPO was an effective biocatalyst in selected organic solvents, such as dichloromethane, dichloroethane and toluene, when catechin was used as a substrate. All data support that B. erythropus has a highly active PPO, possessing similar biochemical and kinetic characteristics to other plant PPOs. (C) 2009 Elsevier Ltd. All rights reserved.