Polyphenol oxidase properties, anti-urease, and anti-acetylcholinesterase activity of Diospyros lotus L. (Plum Persimmon)

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Faiz O., BALTAS N.

INTERNATIONAL JOURNAL OF FOOD PROPERTIES, vol.20, no.5, pp.1186-1196, 2017 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 20 Issue: 5
  • Publication Date: 2017
  • Doi Number: 10.1080/10942912.2016.1205086
  • Journal Name: INTERNATIONAL JOURNAL OF FOOD PROPERTIES
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1186-1196
  • Keywords: Plum persimmon, Affinity column, Enzymatic browning, AChE inhibition, Urease inhibition, PARTIAL-PURIFICATION, DIPHENOLASE ACTIVITIES, BIOLOGICAL-ACTIVITIES, FRUITS, INHIBITION, MONOPHENOLASE, IMPROVEMENT, CULTIVARS, PROTEINS, BINDING
  • Recep Tayyip Erdoğan University Affiliated: Yes

Abstract

Diospyros lotus fruit polyphenol oxidase was purified using affinity chromatography, resulting in a 15-fold enrichment in specific activity. The purified enzyme, having 16.5 kDa molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, exhibited the highest activity toward 4-methylcatechol. Maximum diphenolase activity was reached at pH 7.0 and 60 degrees C in the presence of 4-methylcatechol. K-m and V-max values were calculated as 3.8 mM and 1250 U/mg protein, respectively. Ascorbic acid was a promising inhibitor with an IC50 value of 0.121 mu M. The activity of the purified enzyme was stimulated by Fe2+, Sr2+, Zn2+, and K+ and deeply inhibited by Hg2+, at 1 mM final concentration. Aqueous extract of Diospyros lotus L. fruit showed strong substantial urease and acetylcholinesterase inhibition, with IC50 values of 1.55 +/- 0.05 and 16.75 +/- 0.11 mg/mL, respectively.