α-1,3-Glucanase: present situation and prospect of research

alpha-1,3-Glucanases hydrolyze alpha-1,3-glucan which is an insoluble linear alpha-1,3-linked homopolymer of glucose and these enzymes are classified into two families of glycoside hydrolases on the basis of amino acid sequence similarity; type-71 alpha-1,3-glucanases found in fungi and type-87 enzymes in bacteria. alpha-1,3-Glucan (also called 'mutan') is a major component of dental plaque formed by oral Streptococci and has important physiological roles in various fungal species, including as a component of cell walls, an endogenous carbon source for sexual development, and a virulent factor. Considering these backgrounds, alpha-1,3-glucanases have been investigated from the perspectives of applications to dental care and development of cell-wall lytic enzymes. Compared with information regarding other glycoside hydrolases such as amylases, cellulases, chitinases, and beta-glucanases, there is limited biochemical and structural information available regarding alpha-1,3-glucanase. Further research on alpha-1,3-glucanases on enzyme application to dental care and biological control of pathogenic fungi is expected. In this mini-review, we briefly describe how alpha-1,3-glucanases are categorized and characterized and present our study findings regarding alpha-1,3-glucanase from Bacillus circulans KA-304. Furthermore, we briefly discuss potential future applications of alpha-1,3-glucanases.