Genome Wide Identification and Comparative Analysis of Invertase in Aspergillus spp

Abstract

Invertase is responsible for the hydrolysis of sucrose to glucose and fructose as an inverted sugar. Invertase is important for its various applications in the food, confectionery, and pharmaceutical industries. The current study mainly focuses on genome-wide identification of fungal invertases by doing BLAST and chromosomal mapping. In silico characterization, gene structure analysis, subcellular localization and gene ontology, homology modelling, and RNA seq analysis of Aspergillus fumigatus were performed. To investigate the role of the invertase enzyme in 4 Aspergillus species 16 proteins were identified based on their catalytic domain. This study found that these sixteen proteins are evenly distributed on 2, 5, 6, and 8 chromosomes. Multiple sequence alignment and phylogenetic analysis showed great conservation and evolutionary relationship among invertase proteins. Most of the proteins are found extracellularly present. Gene structure analysis showed the presence of introns and exons structure. Furthermore, RNA sequence analyses were performed in the presence of sugarcane bagasse and fructose to confirm the expression of the invertase enzyme on Aspergillus fumigatus. Results showed that two invertase proteins are found in the expression of two substrates sugar cane bagasse and fructose. Their characterization helped us in understanding the genomic basis of invertases in fungal species. In vitro studies confirmed the presence of invertase enzyme in Aspergillus flavus and Aspergillus fumigatus. Fungal cultures were subjected to submerged fermentation to find out the total units of enzyme produced. and maximum protein estimation of enzyme was obtained. This will provide insights for future applications of invertases in the food and pharmaceutical industries.