PURIFICATION AND PROPERTIES OF MANGANO-SUPEROXIDE DISMUTASE FROM A STRAIN OF ALKALIPHILIC BACILLUS

A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogenei ty from a strain of alkaliphilic Bacillus for the first time. The puri fied protein. with an isoelectric point of pH 4.5, had a molecular mas s of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was r-Ala-Ala-Asn-Ala-Leu-Glu -Pro-His-Ile-Asp-Glu-Ala. The optimum pH and temperature for the react ion were 7.5 and 35 degrees C, respectively. The properties of the sup eroxide dismutase were compared with those of the enzyme from thermoph ilic Bacillus stearothermophilus.