The structural and functional evaluation of amylase activity in Drosophila melanogaster, in comparison to other related insect species: A detailed approach

Abstract

The role of Drosophila melanogaster, or fruit fly, in biological research has been highly remarkable, particularly in genetics and developmental biology. It is a valuable model organism for research for almost a century which holds a significant impact on human health. One of the remarkable features of this organism recently identified is the ability of the larvae to excrete amylase. Amylase, a glycosyl hydrolase is responsible for the degradation of ɑ-1,4 glycosidic bonds in starch molecule to its constituent monosaccharides. The excretion of such a digestive enzyme by Drosophila larvae was predicted to play an important role in the physical softening of food and improvement of efficiency of food ingestion. Apart from Drosophila, certain insects such as bugs, silkworm, honeybee, or even other species of the Drosophila family are known to secrete amylases, which may differ in properties such as optimum pH, temperatures or protein sequences as reported by the presence of several amylase gene copies. Various studies had been performed on the various ‘isozymes’ of such amylases to determine their catalytic activities, similar heat sensitivities, or temporal expressions but the exact role of such enzymes in the human system is yet to be elucidated.