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Fig. 1 | Microbial Cell Factories

Fig. 1

From: Expression, biochemical and structural characterization of high-specific-activity β-amylase from Bacillus aryabhattai GEL-09 for application in starch hydrolysis

Fig. 1

Sequence and structure analysis of AmyBa. A Multiple sequence alignment of β-amylases. The strictly conserved residues are shown on a red background, and the highly conserved residues shown on a yellow background. The secondary structure elements are shown for B. cereus β-amylase (PDB ID: 5BCA). The signal-peptide-cleavage site and two catalytic residues (E) are indicated by black triangles (black inverted triangle). Conservation of the flexible loop motif (HXCGGNVGD) is noted. β-amylase accession numbers are as follows: B. aryabhattai (WP_033580731.1), B. cereus (P36924.2), B. flexus (RIV10038.1), B. firmus (P96513.1), B. circulans (P06547.1), T. thermosulfurigenes (P19584.1). B Three-dimensional molecular model of B. aryabhattai β-amylase (AmyBa). C Superimposition of AmyBa (Blue) and soybean β-amylases (PDB ID: 1Q6C) (gray) and D (PDB ID: 1Q6C) (gray). The C-terminal SBD in microbial β-amylases (box, purple) and the C-terminal loop in plants (box, red)

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Microbial Cell Factories

ISSN: 1475-2859

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