Lyticase from Bacillus subtilis

Lyticase from Bacillus subtilis is a hydrolytic endoglycosidase that specifically cleaves β(1-3)-glucan linkages found in the cell walls and biofilm matrices of fungi and certain bacteria. Lyticase enzyme acts by degrading the structural glucan scaffold of microbial cell walls, enabling the generation of spheroplasts and facilitating nucleic acid extraction from yeast cells.

Lyticase from Bacillus subtilis has been used for:

• digesting yeast cell walls to convert intact cells into spheroplasts enabling subsequent membrane isolation.
• enhancing antimicrobial treatment against interkingdom biofilms when combined with an enzymatic cocktail (cellulase, denarase, and dispersin B) prior to antimicrobial application.

Lyticase cleaves β(1-3) bonds within the glucose units of fungal cell walls and bacterial biofilm matrices, including the Psl polysaccharide of Pseudomonas aeruginosa breaking them down into smaller sugar fragments and dismantling the structural backbone of the cell. It dissolves the yeast (S. cerevisiae) cell wall, measurable as a decrease in optical turbidity at 800 nm (pH 7.5, 25°C). Lyticase requires two components to fully lyse cells: a glucanase that destroys the glucan scaffold, and an alkaline protease that removes the outer mannoprotein layer blocking glucanase access. By breaking down the C. albicans cell wall, lyticase increases permeability and enhances the killing effect of antifungal drugs such as caspofungin.

1U corresponds to the amount of enzyme which decreases the absorbance at 800 nm by 0.001 per minute at pH 7.5 and 25 C (Yeast, Cat. No. 51475, as substrate).