The inhibition effects of some natural products on lactoperoxidase purified from bovine milk

Abstract

In this study, inhibition profiles of some natural products, which are digoxin, L-Dopa, dopamine, isoliquiritigenin, and 1,1,2,2-tetrakis(p-hydroxyphenyl)ethane (Tetrakis), were investigated against bovine lactoperoxidase (LPO) enzyme. Digoxin, L-Dopa, and dopamine are active ingredients of some drugs, which have important functions in our body, especially in cases of heart failure. Isoliquiritigenin and tetrakis are types of natural phenolic compounds, which play an important role in cancer prevention and treatment. LPO enzyme was purified from bovine milk using sepharose-4B-l-tyrosine sulfonamide affinity column chromatography. LPO is responsible for the nonimmune biological defense system and has antibacterial activity so selection of these active substances is important. The inhibition studies are performed with the ABTS substrate. Bovine LPO enzyme was effectively inhibited by phenolic molecules. K values of these natural products were found as 0.20 ± 0.09, 0.22 ± 0.17, 0.49 ± 0.11, 0.49 ± 0.27, and 1.20 ± 0.25 μM, respectively. Tetrakis and digoxin exhibited noncompetitive inhibition, and other molecules showed competitive inhibition.

Lactoperoxidase inhibition of some natural phenolic compounds: Kinetics and molecular docking studies

“…Especially, LPO is a prominent milk enzyme (Sisecioglu, Cankaya, Gulcin, & Ozdemir, 2009, 2010. It catalyzes the oxidation of both organic and inorganic substrates using H 2 O 2 as an oxidant agent (Kohler & Jenzer, 1989;Koksal, Kalin, Gerni, Gulcin, & Özdemir, 2017;Sisecioglu, Uguz, Cankaya, Özdemir, & Gulcin, 2011). Also, it converts bromide (Br − ) and iodide (I − ) ions to hypobromite (BrO -), and hypoiodite (IO -), respectively.…”

Screening of in Vitro Inhibition of Lactoperoxidase Enzyme by Methyl Benzoate Derivatives with Molecular Docking Studies

“…Kinetic tests with varying chemical concentrations and substrate were carried out to study the in vitro inhibitory mechanisms of the analogs (1 a-16 a). [2][3][4] Lineweaver-Burk and IC 50 plots, K i constants, and various types of inhibition were all created using the observed data. [37][38][39][40]…”

“…LPO, a peroxidase isolated from milk, was the first enzyme identified in milk [1,2] . LPO is mostly found in lachrymal glands of mammalians, including sheep, goat, camel, bovine, cow, mouse, buffalo, human, and lama [3,4] . The enzyme's primary tasks include catalyzing the oxidation of compounds in the presence of H 2 O 2 and helping to produce compounds with a variety of antibacterial properties [5,6] .…”

“…[1,2] LPO is mostly found in lachrymal glands of mammalians, including sheep, goat, camel, bovine, cow, mouse, buffalo, human, and lama. [3,4] The enzyme's primary tasks include catalyzing the oxidation of compounds in the presence of H 2 O 2 and helping to produce compounds with a variety of antibacterial properties. [5,6] The secondary substrates for the enzyme are halogens, thiocyanates, or pseudohalogens, all of which have a similar antibacterial effect.…”

Purification and selected biochemical properties of peroxidase from cress (Lepidium sativum sub sp. sativum)

“…The final mixture contained 50 µL enzyme sample, 45 mM guaiacol (1.0 mL), 22.5 mM H 2 O 2 (1.0 mL), and 950 µL phosphate buffer (0.1 M, pH 7.0). [39] Qualitative and quantitative protein determination Bradford method was used for determination of the protein quantity. [40] On the other hand, the qualitative protein amount was measured at 595 nm.…”