Abstract
Mycobacterium tuberculosis (MTB), the main causative organism of tuberculosis (TB), is a successful pathogen that overcomes the numerous challenges presented by the immune system of the host. The situation regarding control of tuberculosis has significantly worsened over the last decade with the spread of strains resistant to multiple antimycobacterial agents. Mycobacterial cell wall has potential as a target for developing protein therapeutic enzybiotic to overcome resistancy case in TB. One of the compiler of mycobacterial cell wall is arabinogalactan which is compiled by arabinose with unusual stereochemical. α-L-arabinofuranosidase (Abfa) is an enzyme that can breakdown arabinofuranosidic bond. However, its ability to breakdown the arabinofuranosidic from D-arabinose as monomer is still unknown. Here we present protein engineering through computational design to improve the specificity of Abfa by replacing discriminate amino acid residue. The effort is done to analyze the ability of Abfa in hydrolyzed mycobacterial cell wall and also to analyze the anti-TB assay of Abfa.
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