IN SILICO ANALYSIS AND FUNCTIONAL CHARACTERIZATION OF PHYTASE ENZYME FROM BACILLUS AMYLOLIQUEFACIENS

Abstract

Phosphorus is an essential nutrient for the growth of plants and serves as the backbone for vital molecules essential for their survival. However, it exists in insoluble organic and inorganic forms in soils, resulting in limited availability to plants. Within the rhizosphere, phosphate-mineralizing bacteria facilitate the transformation of insoluble organic phosphorus into a plant-accessible form through the release of phytase enzymes. Phytase enzyme generates phosphorus by breaking down phytate. Numerous bacteria, including Bacillus species, have been identified to secrete phytases and play key role in phytate-phosphorus cycling. Therefore, this study conducted a comprehensive in silico analysis focusing on both the structural and functional attributes of the phytase enzyme in Bacillus spp. The research explored correlations by examining the phylogenetic relationship among phytase enzyme of various Bacillus species and strains. Physicochemical properties and STRING analysis were also investigated using diverse bioinformatics tools. B. amyloliquefaciens was chosen as the representative species for the 3D modeling of the phytase enzyme. The phytase protein demonstrated an average molecular weight of approximately 41.75 kDa, displaying a high percentage of beta turns and strands in its secondary structure, indicating thermal stability. This theoretical evaluation of the structure and function of phytase-producing Bacillus could assist researchers in gaining a better understanding of their potential for phytate hydrolysis. Furthermore, it might facilitate the elucidation of the catalytic activity and selection of phytase variants with desired characteristics.