Enhanced production and biochemical characterization of a thermostable amylase from thermophilic bacterium Geobacillus icigianus BITSNS038

The current study focuses on optimizing, characterizing, and purifying a thermostable amylase from thermophilic bacteria Geobacillus icigianus (BITSNS038). The amylase was produced optimally at 18-24 h of incubation in the presence of starch and tryptone at 7.5 and 3.0 g/L, respectively (pH 7.0, 70 degrees C, and 150 rpm). K-m, V-max values for starch were 2.17 mg/mL and 4.16 U/mL respectively. The enzyme showed excellent thermal stability at 70 degrees C, retaining 62.5% residual activity after 8 h and a reduced deactivation rate constant (k(d)) of 0.001. When tested for its efficacy in starch hydrolysis, it showed 34.5% hydrolysis of corn starch slurry and antibiofilm activity, but no antimicrobial activity was noticed. The ultrafiltration led to partial purification of amylase showed 2.67-fold purification with a molecular weight in the range of 45 and 66 kDa. This is probably the first-ever report on a thermostable amylase from G. icigianus and its extensive potential uses.