Purification and Biochemical Characterization of Phytase Enzyme from Lactobacillus coryniformis (MH121153)

Molecular Biotechnology
Yeliz DemirŞükrü Beydemir

Abstract

Phytase (myo-inositol hexaphosphate phosphohydrolase) belongs to phosphatases. It catalyzes the hydrolysis of phytate to less-phosphorylated inorganic phosphates and phytate. Phytase is used primarily for the feeding of simple hermit animals in order to increase the usability of amino acids, minerals, phosphorus and energy. In the present study, phytase isolation from the Lactobacillus coryniformis strain, isolated from Lor cheese sources, phytase purification and characterization were studied. The phytase was purified in simple three steps. The enzyme was obtained with 2.60% recovery and a specific activity of 202.25 (EU/mg protein). The molecular mass of the enzyme was determined to be 43.25 kDa with the sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The optimum temperature and pH for the enzyme were found as 60 °C and 5.0 and respectively. To defined the substrate specificity of the phytase, the hydrolysis of several phosphorylated compounds by the purified enzyme was studied and sodium phytate showed high specificity. Furthermore, the effects of Ca2+, Ag+, Mg2+, Cu2+, Co2+, Pb2+, Zn2+ and Ni2+ metal ions on the enzyme were studied.

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Citations

Jun 11, 2019·Drug and Chemical Toxicology·Şükrü BeydemirAhmet Yalçın
Mar 24, 2020·Archives of Physiology and Biochemistry·Yeliz Demir, Zeynep Köksal
Feb 19, 2020·Anti-cancer Agents in Medicinal Chemistry·Yeliz DemirŞükrü Beydemir
Sep 13, 2020·Biotechnology and Applied Biochemistry·Fazilet Parlakova KaragözNeslihan Dikbaş
Nov 13, 2019·Applied Microbiology and Biotechnology·Hanchi ChenYuele Lu
Aug 14, 2020·Journal of Biomolecular Structure & Dynamics·Cüneyt TürkeşŞükrü Beydemir
Jan 16, 2021·Journal of Basic Microbiology·Sergio H Sandez PenidezGraciela C Rollán
Nov 15, 2021·Biotechnology and Applied Biochemistry·Cansu ÖztürkÖmer İrfan Küfrevioglu

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