Phytases and phosphatases of thermophilic microbes: Production, characteristics and multifarious biotechnological applications

Abstract

Thermophilic microbes have been considered as good sources of-thermostable enzymes with high catalytic activity, greater resistance to denaturing agents and lower incidence of contamination. Thermostable enzymes are receiving considerable attention because of their usefulness in high-temperature catalysis of various enzymatic industrial processes. Phytases (myo-inositol hexakisphosphate phosphohydrolase) are the phosphatases, which catalyse the hydrolysis of phytic acid to inorganic phosphate and myo-inositol phosphate derivatives, while phosphatases are able to hydrolyse a wide variety of esters and anhydride phosphoric acids, releasing phosphate, and are also able to perform transphosphorylation reactions. The phosphorus thus liberated is used in metabolic pathways. The phosphatases have been considered to be one of the most versatile groups of hydrolases because of their adaptability under different environmental extremes such as high-temperature regimes and regulate phosphate metabolism for maintaining phosphorus economy of the cell for fulfilling its growth as well as bioenergetic requirements. The reduction of phytic acid content in the foods and feeds by enzymatic hydrolysis using phytase is desirable, because the physical and chemical methods of phytate removal negatively affect their nutritional value. These enzymes, therefore, have potential applications in food and feed industries for mitigating their phytic acid content to liberate available inorganic phosphate and improve digestibility as a result of elimination of antinutrient characteristics. In this review, the attention is focused on the production, characteristics and potential biotechnological aspects of phytases and phosphatases from thermophilic microbes.