Romanian Biotechnological Letters Vol. 20, No. 6, 2015
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ORIGINAL PAPER
Romanian Biotechnological Letters, Vol. 20, No. 6, 2015 10961
Inhibition of Polyphenol Oxidase Purified from Potato
(Solanum tuberosum)
Received for publication, March 9, 2015
Accepted, August 7, 2015
HATICE AYSUN MERCIMEK*, GULCIHAN GUZELDAG, FILIZ UCAN,
KIVILCIM CAKTU GULER, MUHAMMET KARAMAN, RAMAZAN KARAYILAN
Department of Moleculer Biology and Genetics, Kilis 7 Aralık University, 79000,
Kilis,Turkey.
*Address correspondence to: “Kilis 7 Aralık University, The Faculty of Sciences and
Letters, Department of Molecular Biology and Genetics, Kilis, Turkey’’
Tel.: +90 348 822 23 50/1452; Fax: +90 348 822 23 51,
*
Corresponding author: Email: mersimek@hotmail.com
Abstract
Enzymatic browning reaction caused by polyphenol oxidases (PPOs) due to negative effects on
sensorial and nutritional quality of plants, is one of the most important problem in food industry.
This study was designed for characterization and purification of PPO from potato and to determine
the inhibitory activity of methanolic extracts of Citrus sp., (lemon) Beta vulgaris (red beet) and
Capsicum sp. (chili pepper) on PPO. The molecular weight of partial purified PPO, its enzyme activity
against catechol substrat and the amount of total protein in sample were determined as 40 kDa,
1340 EU mL
-1
and 433 μg mL
-1
, respectively. The characteristic peaks of PPO were clearly observed in
FTIR spectra. According to spectrophotometric analyses, it was found that PPO activity inhibition by
extracts of chili pepper, lemon and red beet was in the rate of 70, 54 and 60%, respectively. Ascorbic
acid content of chili pepper was determined as 143.85 mg 100 g
-1
. Out of the three extracts, the chili
pepper extract was determined to show the maximum anti-browning effect. In various industrial
areas such as food industry, health care and medicine to cure skin disorders, extracts of natural
vegetables as an alternative to synthetic PPO inhibitors could be used to prevent enzymatic
browning reaction.
Keywords: Enzymatic browning, polyphenol oxidase, Solanum tuberosum, inhibition, FTIR
1. Introduction
Polyphenol oxidase (PPO) known as phenolase, tyrosinase, monophenol, o-diphenol:
oxygen oxidoreductase and EC 1.14.18.1, is a member of oxidoreductases (1-4). PPO, is a
group of copper enzymes that catalyzes the oxidation of phenolic compounds by two different
reactions by using molecular oxygen as a co-substrate: the hydroxylation of monophenols to o-
diphenols, (monophenolase or cresolase activity) and the subsequent oxidation of o-diphenols to
o-quinones (diphenolase or catecholase activity) that are reddish-brown pigments (1-2, 5-8).
This enzyme is widely found in organisms including plant, fungi, animal and bacteria (2).
When a plant encounters with cell-damaging treatments such as crushing, cutting and
decay, PPO, located in the plastids of plant cells, may contact with certain phenolic
substrates, stored in the vacuoles, leading to browning (1-2, 9-10). As a result of this defense