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

• DOI: 10.1007/s11274-011-0715-5
• Publication Date: 2011-03-26T14:29:22Z
• Authors: Ilaria Finore; Ceyda Kasavi; Annarita Poli; Ida Romano; Ebru Toksoy Oner; Betul Kirdar; Laura Dipasquale; Barbara Nicolaus; Licia Lama
• Keywords: 0106 biological sciences; Alpha-amylase; amyA gene sequence; Geobacillus thermoleovorans subsp. stromboliensis; Raw-starch-digestion; Thermostability; 01 natural sciences

characterization of a rawstarch-digesting a-amylase from Geobacillus thermoleovorans subsp. stromboliensis subsp. nov. (strain PizzoT). The molecular weight was estimated to be 58 kDa by SDS-PAGE. The enzyme was highly active over a wide range of pH from 4.0-10.0. The optimum temperature of the enzyme was 70C. It showed extreme thermostability in the presence of Ca2?, retaining 50%of its initial activity after 90 h at 70C. The enzyme efficiently hydrolyzed 20% (w/v) of raw starches, concentration normally used in starch industries. The a-amylase showed an high stability in presence of many organic solvents. In particular the residual activity was of 73% in presence of 15% (v/v) ethyl alcohol, which corresponds to ethanol yield in yeast fermentation process. By analyzing its complete amyA gene sequence (1,542 bp), the enzyme was proposed to be a new a-amylase.