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

SANDEZ PENIDEZ, SERGIO H.; VELASCO MANINI, MARINA A.; GEREZ, CARLA L.; ROLLÁN, GRACIELA C.

JOURNAL OF BASIC MICROBIOLOGY

WILEY-V C H VERLAG GMBH

Año: 2020 vol. 60 p. 787 - 798

0233-111X

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), anantinutritional compound with the ability to chelate cations and proteins.Phytase is an enzyme that catalyzes the hydrolysis of IP6 and it is used as anadditive improving the nutritional quality of grain‐based foods. The aim of thisstudy was to select lactic acid bacteria (LAB) isolated from pseudocereals withphytase activity, characterize their production and activity, and purify theenzyme. LAB strains isolated from grains and spontaneous sourdough ofquinoa and amaranth were grown in the Man Rogosa and Sharpe mediumwhere the inorganic phosphate (Pi) was replaced by 1% of IP6. Phytase activitywas determined by measuring the Pi released from IP6. Phytase of Lactobacillus(L.) plantarum CRL1964 (PhyLP) showed the highest specific activityfrom 73 LAB evaluated. IP6 induces PhyLP production, which is at its maximumat the end of the exponential phase. PhyLP was thermostable andmaintained its activity under acidic conditions. The enzymatic activity is stimulatedby ethylenediaminetetraacetic acid, Co2+, and ascorbic acid. PhyLPwas partially purified and showed a molecular mass of 55 kDa. L. plantarumCRL1964 and/or PhyLP have the potential to be included in the processing ofcereal/pseudocereals based products for animal feed and/or the food industryimproving its nutritional value.