Objective:
Amylases enzymes hydrolyze starch molecules to produce diverse products including
dextrins, and progressively smaller polymers. These include glucose units linked through α-1-
1, α-1-4, α-1-6, glycosidic bonds.
Methods:
This enzyme carrying an (α /β) 8 or TIM barrel structure is also produced containing the catalytic
site residues. These groups of enzymes possess four conserved regions in their primary sequence.
In the Carbohydrate-Degrading Enzyme (CAZy) database, α-amylases are classified into different
Glycoside Hydrolase Families (GHF) based on their amino acid sequence. The present objective
was to study one such enzyme based on its molecular characterization after purification in our laboratory.
Its main property of solid-natural starch degradation was extensively investigated for its pharmaceutical/
industrial applications.
Results:
Amylase producing bacteria Bacillus cereus sm-sr14 (Accession no. KM251578.1) was purified
to homogeneity on a Seralose 6B-150 gel-matrix and gave a single peak during HPLC. MALDITOF
mass-spectrometry with bioinformatics studies revealed its significant similarity to α/β hydrolase
family. The enzyme showed an efficient application; favourable Km, Vmax and Kcat during the catalysis
of different natural solid starch materials. Analysis for hydrolytic product showed that this enzyme
can be classified as the exo-amylase asit produced a significant amount of glucose.
Conclusion:
Besides the purified enzyme, the present organism Bacillus cereus sm-sr14 could degrade
natural solid starch materials like potato and rice up to the application level in the pharmaceutical/ industrial
field for alcohol production.
Salt-triggered Active Plasmonic Systems Based on the Assembly/Disassembly of Gold Nanorods in a DNA Brush Layer on a Solid Substrate
