Fig. 7.

Sequence alignment of A. flavus NSH9 α-amylase with two other proven raw starch degrading fungal α-amylase to date (Cryptococcus sp. S-2 Accession no: BAA12010.1; Saccharomycopsis fibuligera Accession no: ADD80242.1) as compared to α-amylase of proven crystal structure (Human pancreatic α-amylase PDB-5TD4; Human saliva α-amylase PDB-1SMD; Barley α-amylase PDB-1RPK; A. niger NSH9 α-amylase PDB-2GUY). Amino acids in red indicate GH13 family catalytic domain; in blue indicate domain of unknown function/α-amylase C-terminal domain; and in green indicate CBM20. α-amylase surface/secondary-binding sites (SBS) residues from human saliva and pancreatic were shown in bold and highlighted in green and blue; SBS from barley were shown in bold and highlighted yellow, while maltose-binding sites from A. niger were shown in bold and highlighted in grey