Biochemical and in Silico Structural Characterization of a Cold-Active Arginase from the Psychrophilic Yeast, Glaciozyma Antarctica PI12

Glaciozyma antarctica PI12 is a psychrophilic yeast isolated from Antarctica. In this work, we describe the heterologous production, biochemical properties and in silico structure analysis of an arginase from this yeast (GaArg). GaArg is a metalloenzyme that catalyses the hydrolysis of l-arginine to l-ornithine and urea. The cDNA of GaArg was reversed transcribed, cloned, expressed and purified as a recombinant protein in Escherichia coli. The purified protein was active against l-arginine as its substrate in a reaction at 20 °C, pH 9. At 10–35 °C and pH 7–9, the catalytic activity of the protein was still present around 50