Partial characterization and purification of phytase from Lactobacillus plantarum CRL1964 isolated from pseudocereals

Abstract

Cereals and pseudocereals are a rich source of nutrients and trace elements, but their dietary bioavailability is low due to the presence of phytate (IP6), an antinutritional compound with the ability to chelate cations and proteins. Phytase is an enzyme that catalyzes the hydrolysis of IP6 and it is used as an additive improving the nutritional quality of grain-based foods. The aim of this study was to select lactic acid bacteria (LAB) isolated from pseudocereals with phytase activity, characterize their production and activity, and purify the enzyme. LAB strains isolated from grains and spontaneous sourdough of quinoa and amaranth were grown in the Man Rogosa and Sharpe medium where the inorganic phosphate (Pi) was replaced by 1% of IP6. Phytase activity was determined by measuring the Pi released from IP6. Phytase of Lactobacillus (L.) plantarum CRL1964 (PhyLP) showed the highest specific activity from 73 LAB evaluated. IP6 induces PhyLP production, which is at its maximum at the end of the exponential phase. PhyLP was thermostable and maintained its activity under acidic conditions. The enzymatic activity is stimulated by ethylenediaminetetraacetic acid, Co2+, and ascorbic acid. PhyLP was partially purified and showed a molecular mass of 55 kDa. L. plantarum CRL1964 and/or PhyLP have the potential to be included in the processing of cereal/pseudocereals based products for animal feed and/or the food industry improving its nutritional value.