Purification and properties of a new, commercial, thermostableBacillus stearothermophilusα‐amylase

Purification, biochemical characterization and gene sequencing of a thermostable raw starch digesting α-amylase from Geobacillus thermoleovorans subsp. stromboliensis subsp. nov.

“…However, under native conditions (gel filtration chromatographySuperdex S 200) the enzyme eluted at an apparent MW of 28 kDa. Variable apparent molecular weights have also been observed for amylases produced by B. stearothermophilus, B. brevis, Streptococcus bovis and Clostridium acetobutylicum which was generally attributed to the interactions of the enzymes with gel filtration matrices, composed of glucose polymers, resulting in retarded elution as also observed in this study (Brumm et al 1988). …”

Characterization of Amylolytic Enzymes, Having Both α-1,4 and α-1,6 Hydrolytic Activity, from the Thermophilic Archaea Pyrococcus furiosus and Thermococcus litoralis

“…(24), and C. thermohydrosulfuricum (31). The thermal stability of a-amylases is also typically enhanced by Ca2+ (5,14). The reasons for these effects are not known, although metal ions often act as salt or ion bridges between two adjacent amino acids.…”