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.

Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus brevis Isolated from Fresh Kashar Cheese

“…Karagöz et al [11] reported the protein concentration of phytase purified from L. plantarum as 0.11 mg/mL. Sandez Penidez et al [26] reported the protein value of phytase enzyme partially purified from L. plantarum as 0.08 mg/mL. Demir et al [22] determined the protein amount of phytase purified from L. coryniformis as 0.12 mg/mL in their study.…”

“…Dikbaş et al [8] determined the pH and temperature at which the phytase enzyme partially purified from L. brevis showed optimum activity as pH 3.0 and 60 °C, respectively. Sandez Penidez et al [26] found that L. plantarum CRL1964 (PhyLP) phytase exhibited optimum activity at pH 4.5 and 55°C. Based on the literature studies and the findings obtained, it is seen that the phytase enzyme purified from Lactobacillus spp.…”

Biochemical properties of phytase immobilized and its effect on growth parameters of tomato

“…In the present study, phytase purified from L. kefiri (approx. 72 kDa) was found to have a higher molecular weight than Lactobacillus coryniformis (43.25 kDa) (Demir et al., 2018), L. plantarum CRL1964 (55 kDa) (Sandez Penidez et al., 2020), and L. brevis (49.9 kDa) (Dikbaş, Uçar, et al., 2023) and a similar molecular weight to L. plantarum (72 kDa) (Sumengen et al., 2013), L. brevis (73 kDa) (Sümengen et al., 2012), and L. paracasei (70 kDa) (Bhagat et al., 2019). Considering the literature studies and the results obtained, it is seen that the molecular weight of purified phytases can vary according to their source.…”

Toward Sourdough Microbiome Data: A Review of Science and Patents

“…The main fermentation products generated by sourdough microbiota are mostly related to sensory attributes, such as volatile and phenolics compounds, and organics acids [44,[55][56][57][58]; however, some researchers have also found phytase, γ-aminobutyric acid (GABA), antioxidant and anti-inflammatory compounds, thus associating sourdough consumption with potential health benefits [41,56,[59][60][61][62].…”