Journals / Iğdır Üniversitesi Fen Bilimleri Enstitüsü Dergisi / 2018 / Cilt: 8 - Sayı: 2
Lactoperoxidase Enzyme Purified from Different Milk Sources: Inhibition Profile of Capsaicin and Pyrogallol
- Pages
- 159–165
- DOI
- —
Abstract
Peroxidases (POD) have an important use in metabolic functions, enzymatic reactions and clinicaldiagnoses, especially in the food and pharmaceutical industry. Mammalian POD enzymes, Lactoperoxidase (LPO)(hydrogen peroxide oxidoreductase E.C. 1.11.1.7) is localized in milk, saliva and tears, while myeloperoxidase islocalized in leukocytes and platelets. LPO enzyme catalyses the conversion of hypothiocyanate with antibacterialproperties of thiocyanate in the presence of hydrogen peroxide. The purpose of this study was to determine the invitro inhibition effects of capsaicin and pyrogallol on LPO enzyme purified from different milk sources (Bovine,buffalo, sheep and goat). To determine the inhibition effects of capsaicin and pyrogallol on LPO, LPO enzymewas purified from different mammalian milk and then, Lineweaver-Burk graphs were drawn for each inhibitorby measuring enzyme activities; Ki values and inhibition types were determined from these plotted graphs. TheKi values of capsaicin and pyrogallol were found in ranging of 0.0035-36.178 µM. Pyrogallol was shown themost effective inhibitor feature with a non-competitive inhibition type with 0.0035 ± 0.0012 μM Ki value on LPOenzyme purified from sheep milk.
Özet
Peroksidazlar (POD), gıda ve ilaç endüstrisi başta olmak üzere metabolik fonksiyonlar, enzimatik