Purification and characterization of a approximately 34 kDa antioxidant protein (beta-turmerin) from turmeric (Curcuma longa) waste grits.

Abstract:

:Beta-turmerin from turmeric (Curcuma longa) waste grits obtained after extraction of curcumin was purified by successive gel permeation chromatography. Homogeneity of beta-turmerin was confirmed by its movement as single band both in SDS-PAGE and as well as in native (basic) PAGE. The apparent molecular mass is approximately 34 kDa by SDS-PAGE. It is more hydrophobic protein and showed sharp single peak in RP-HPLC with retention time of 62.17 min. It is a glycoprotein as it shows the presence of amino sugars up to 0.021 gm%. In three different model systems i.e., linolenic acid micelles, erythrocyte membrane systems and liposomes, beta-turmerin at 0.125 microM offered 70%, 64%, and 60% inhibition of lipid peroxidation, which is 3200 times more efficient than the standard antioxidants BHA (400 microM) and alpha-tocopherol (400 microM). beta-turmerin inhibited diene-triene and tetraene conjugation up to 54%, 72% and 47%, respectively. beta-turmerin also effectively scavenges hydroxyl radicals when compared to BHA and alpha-tocopherol. beta-turmerin (2.5 microM) further inhibited the activation of PMNL mediated by fMLP up to the extent of 75%, where as standards BHA (400 microM) and mannitol (10 microM) inhibited the same to 65% and 55%, respectively. At 0.125 microM dose beta-turmerin prevented t-BOOH induced cell death at all time intervals. In addition to the above properties, it is non-toxic to lymphocytes as it did not affect the viability of cells. The mechanism of antioxidant action of beta-turmerin could probably be by counteracting/quenching of reactive oxygen species (ROS). We report the purification and characterization of beta-turmerin ( approximately 34 kDa), a potent antioxidant protein from turmeric waste grits.

journal_name

Biochimie

journal_title

Biochimie

authors

Smitha S,Dhananjaya BL,Dinesha R,Srinivas L

doi

10.1016/j.biochi.2009.06.006

subject

Has Abstract

pub_date

2009-09-01 00:00:00

pages

1156-62

issue

9

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(09)00162-X

journal_volume

91

pub_type

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