Isolation of Mutants Defective in α-Amylase from Bacillus subtilis : Genetic Analyses

Isolation, Optimization and Characterization of α- Amylase from Bacillus alcalophilus

Amylase is one of the most important enzymes widely used in paper, textile, pharmaceutical industries etc. In the present investigation a thermostable, alkalophilic amylase was isolated from underlying soil samples of domestic wastes, and was screened on starch agar medium. The amylase activity was measured using colorimetric method at 540nm. Among forty five isolates, thirteen demonstrated cle...

Bottleneck in secretion of α-amylase in Bacillus subtilis

Amylase plays an important role in biotechnology industries, and Gram-positive bacterium Bacillus subtilis is a major host to produce heterogeneous α-amylases. However, the secretion stress limits the high yield of α-amylase in B. subtilis although huge efforts have been made to address this secretion bottleneck. In this question-oriented review, every effort is made to answer the following que...

Heterologous expression, biochemical characterization, and overproduction of alkaline α-amylase from Bacillus alcalophilus in Bacillus subtilis

BACKGROUND Alkaline α-amylases have potential applications for hydrolyzing starch under high pH conditions in the starch and textile industries and as ingredients in detergents for automatic dishwashers and laundries. While the alkaline α-amylase gains increased industrial interest, the yield of alkaline α-amylases from wild-type microbes is low, and the combination of genetic engineering and p...

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

Mutants of Bacillus subtilis

Enzyme activities of glycolysis and glyconeogenesis are present in spores of Bacillus subtilis, the rate-limiting step of glucose (GLC) metabolism being its phosphorylation. GLC allows initiation of germination in the presence of fructose (FRU) and asparagine (ASN), not because it is used via the EmbdenMeyerhof path, but because it is oxidized in the nonphosphorylated form via the spore-specifi...