IN VITRO EVALUATION OF PARTIALLY PURIFIED ANTIOXIDANT ENZYMES FROM LICHEN LEPTOGIUM PAPILLOSUM

Abstract

ABSTRACT
Objective: In this study, the enzyme activity of the partially purified six different antioxidant enzymes (AEs) of Leptogium papillosum such as
superoxide dismutase (SOD), catalase (CAT), peroxidase (POD), polyphenol oxidase (PPO), glutathione transferase (GST), and glutathione peroxidase
(GPx) was carried out.
Methods: Ammonium sulfate precipitation, dialysis, and DEAE-cellulose column chromatography were the three different methods performed to
purify the six different AEs from L. papillosum. The antioxidant enzyme activity of the purified extracts was determined in vitro by the following
standard procedure of SOD, CAT, POD, PPO, GST, and GPx.
Results and Conclusion: The results revealed that there was a significant increase (p<0.001) in the specific activity of purified fractions of all the
enzymes with a corresponding increase in the purification fold. The comparable activity of PPO and GST were determined using cluster analysis using
short linkage distance. Principal component analysis indicated that SOD
contributed primarily to the total variation in the AEs among all
the other fractions with the specific activity of 21.70 U/mg by attaining the purification fold of 5.91. Thus, our findings suggested that the purified
AEs of L. papillosum possess potent antioxidant defense machinery by scavenging free radical population. Moreover, SOD was played a major role of
capturing free radical by having highest enzyme activity followed by GST and CAT.
DEAE-cellulose
Keywords: Antioxidant enzymes, Cluster analysis, DEAE-cellulose column chromatography, Lichen, Leptogium papillosum, Principal component
analysis.