Purification and characterization of polyphenol oxidase from purslane
Yükleniyor...
Tarih
2017
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Sociedade Brasileira de Ciencia e Tecnologia de Alimentos, SBCTA
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
The polyphenol oxidase (PPO) is an enzyme that is responsible for the enzymatic browning of fruits and vegetables. This is generally undesired process and need to be prevented in food technology. PPO from purslane was purified, characterised and the kinetic parameters for three substrates namely, catechol, L-Dopa and 4-methylcatechol were determined. The optimum pH and temperature values were found to be pH 7.0 and 50 °C, respectively using the catechol as substrate. The apparent molecular weight of the PPO from purslane was determined as high as 163 kDa by partially denaturing SDS-PAGE. Moreover, the inhibition kinetics of the purified PPO were determined, using both synthetic and natural inhibitors. Among inhibitors tested, ascorbic acid was the most effective inhibitor with the lowest Ki value of 0.36 mM. This is the first study on the purification and characterisation of PPO from purslane (Portulaca oleracea) that may provide new insight into how to overcome the enzymatic browning.
Açıklama
Anahtar Kelimeler
Inhibitors, Kinetics, Polyphenol oxidase, Portulaca oleracea, Purification
Kaynak
Food Science and Technology (Brazil)
WoS Q Değeri
Q3
Scopus Q Değeri
Q2
Cilt
37
Sayı
3
Künye
Güven, R. G., Güven, K., Bekler, F. M., Acer, Ö., Alkan, H. ve Doğru, M. (2017). Purification and characterization of polyphenol oxidase from purslane. Food Science and Technology (Brazil), 37(3), 356-362.
