Bioinformatics Analysis of α-Amylase Three-Dimensional Structure in Aspergillus oryzae

The major aim of this study is to introduce bimolecular structures from a bioinformatic perspective and informs about the bioinformatic softwares in this field. Each protein has a specific chemical or structural function, strongly suggesting that each has a unique three-dimensional structure. In this study, we investigated α-amylases in Aspergillus oryzae. Among starch converting enzymes, the α-amylases (endo-1, 4-α-D-glucan glucanohydrolase [E.C.3.2.1.1]) are of special importance and extensively studied. PDB and NCBI databases and Chimera, Predict Protein and Multalign softwares used for this research. By using these softwares, multiple analyses, including determination of residue composition, secondary structures, conserved regions, ligand binding site done. Starch-hydrolyzing enzymes such as amylases, pullulanases and glucoamylases play an important role in food, chemical, and pharmaceutical industries. In the certain applications like detergent and bakery industries the properties of α-amylase needed is quite challenging Using of bioinformatic softwares improves our understanding about proteins 3D structures and their functions.

Author(s): Javad Sharifi-Rad, Fatemeh Taktaz and Seyedeh Mahsan Hoseini-Alfatemi

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