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Article 2023 · 5 citations

Purification of phytase enzyme from <i>Lactobacillus brevis</i> and biochemical properties

Dikbas, Neslihan, Ucar, Sevda, Alim, Seyma

Abstract

In this study, Lactobacillus brevis isolated from kashar cheese was identified by 16s rRNA method, phytase enzyme from bacteria was partially purified and characterized. Work continued in two directions. The first step was the isolation and identification of the bacteria. In the second step, the phytase enzyme from L. brevis was partially purified and the optimum pH and temperature values of the purified enzyme were determined. The phytase activity of the identified L. brevis was determined as 212.97 U/mL. The molecular mass of the enzyme was determined as 49.9 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) method. The K-m and V-max values for sodium phytate were 0.0154 mM and 2.00 mu mol/min, respectively. The optimum pH and temperature values of partially purified phytase were determined as pH 3.0, 60 degrees C, respectively.

Keywords
Lactobacillus brevis Phytase 16s rRNA LACTIC-ACID BACTERIA THERMOSTABLE PHYTASE SOURDOUGH FOOD
WoS Categories
Biology
Sustainable Development Goals
Citation
Journal
BIOLOGIA
Year
2023
Volume
78
Issue
9
Pages
2583-2591
ISSN
0006-3088
eISSN
1336-9563
DOI
10.1007/s11756-023-01403-9
WoS UID
WOS:000968182700001
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