ANTIOXIDANT POTENTIAL OF ORAL FEEDING OF CYNODON DACTYLON EXTRACT ON DIABETES-INDUCED OXIDATIVE STRESS

The present study is an extension of our previous research work and it deals with the scientific evaluation of antioxidant potential of the aqueous extract of Cynodon dactylon on diabetes-induced oxidative stress of diabetic rats. The most effective dose of 500 mg/kg of extract was given orally to diabetic rats for 30 days. Different oxidative stress parameters were analyzed in various tissues of control and treated diabetic rats. The observed elevated level of LPO comes down significantly ( P <  0.05), and decreased activities of antioxidant enzymes such as CAT, SOD, GPx and GST got increased ( P <  0.05) significantly in diabetic rats on extract treatment. The flavonoids present in the aqueous extract of this plant might be responsible for its marked antioxidant efficacy at tissue level in STZ-induced diabetic rats.

PRACTICAL APPLICATIONS

The Cynodon dactylon has been shown to possess varied medicinal properties. The aqueous extract of the rhizome is used as anti-inflammatory, diuretic, antiemetic, antidiabetic and blood-purifying agent. Recently, it has been reported by our research group that the extract of C. dactylon has hypoglycemic as well as antidiabetic potential. The present communication is an endeavor in the direction of evaluating its in vivo antioxidant effect in STZ-induced diabetic rats so that it can be used as a value-added agent for managing diabetes as well as oxidative stress associated with it.     

ALPHA-GALACTOSIDASE OF GERMINATING SEEDS OF CASSIA SERICEA SW.

Germinating seeds of Cassia sericea Sw. contain two molecular forms of α-galactosidase which were partially purified and characterized. Both enzyme forms had an optimum pH of 5.0 and an optimum temperature of 50 °C. K_m values for the substrate p-nitrophenyl-α-D-galactoside (PNPG) were 0.91 mM and 1.05 mM for the two forms, and substrate inhibition was observed at high concentrations of PNPG. The two forms of the enzyme had molecular weights of 46,000 and 33,000 by gel filtration. The enzyme forms were inhibited completely by Ag⁺, Cu²⁺ and Hg²⁺ ions and by p-chloromercuribenzoate showing that thiol groups are probably involved in catalysis. Both α-galactosidases hydrolyzed melibiose and raffinose, although hydrolysis of stachyose could not be detected. The enzyme may find potential use in the food industry to hydrolyze flatulence-causing sugars in processed foods and in production of sucrose from high-raffinose sugar beets. That the source (C. sericea seeds) of the enzyme is inexpensive provides an added advantage over use of cultivated legumes as a source of α-galactosidase.