Identification of α-amylase gene by PCR and activity of thermostable α-amylase from thermophilic Anoxybacillus thermarum isolated from Remboken hot spring in Minahasa, Indonesia

Purification and characterization of extracellular α-amylase from a thermophilic Anoxybacillus thermarum A4 strain

α-Amylase from Anoxybacillus thermarum A4 was purified using ammonium sulphate precipitation and Sephadex G-100 gel filtration chromatography, with 29.8-fold purification and 74.6% yield. A4 amylase showed best performance for soluble potato starch hydrolysis at 70 °C and pH 5.5-10.5. A4 amylase was extremely stable at +4 °C, and the enzyme retained over 65% of its original α-amylase activity a...

Thermophilic Bacillus Licheniformis Rbs 5 Isolated from Hot Tunisian Spring Co-producing Alkaline and Thermostable Α-amylase and Protease Enzymes

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

Purification and Characterization of Thermostable and Detergent-Stable α-Amylase from Anoxybacillus sp. AH1.

A thermostable and detergent-stable α-amylase from a newly isolated Anoxybacillus sp. AH1 was purified and characterized. Maximum enzyme production (1874.8 U/mL) was obtained at 24 h of incubation. The amylase was purified by using Sephadex G-75 gel filtration, after which an 18-fold increase in specific activity and a yield of 9% were achieved. The molecular mass of the purified enzyme was est...

Production of Thermostable α-Amylase and Cellulase from Cellulomonas sp

A bacterium, isolated from rabbit’s waste and identified as Cellulomonas sp., had cellulase and thermostable α-amylase activity when grown on wheat bran. Maximum activity of thermostable α-amylase was obtained by adding 3% soluble starch. However, soybean oil (1 ml l) could increase the production of α-amylase and cellulase in wheat bran. The α-amylase was characterized by making a demonstratio...