Purification of phytase enzyme from Lactobacillus brevis and biochemical properties

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DİKBAŞ N., Uçar S., Alım Ş.

Biologia, vol.78, no.9, pp.2583-2591, 2023 (SCI-Expanded)

• Publication Type: Article / Article
• Volume: 78 Issue: 9
• Publication Date: 2023
• Doi Number: 10.1007/s11756-023-01403-9
• Journal Name: Biologia
• Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Animal Behavior Abstracts, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Veterinary Science Database
• Page Numbers: pp.2583-2591
• Keywords: Lactobacillus brevis, Phytase, 16s rRNA, LACTIC-ACID BACTERIA, THERMOSTABLE PHYTASE, SOURDOUGH, FOOD
• Ataturk University Affiliated: Yes

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 Km and Vmax values for sodium phytate were 0.0154 mM and 2.00 µmol/min, respectively. The optimum pH and temperature values of partially purified phytase were determined as pH 3.0, 60 °C, respectively.