A novel purple acid phytase from an earthworm cast bacterium. (19th February 2018)

• Record Type: Journal Article
• Authors: Ghorbani Nasrabadi, Reza; Greiner, Ralf; Yamchi, Ahad; Nourzadeh Roshan, Elham
• Is Part Of: Journal of the science of food and agriculture. Volume 98:Number 10(2018)
• Page Start: 3667
• Page End: 3674
• Publication Date: 2018-02-19
• Subjects: phytase -- earthworm -- HPIC -- myo‐inositol phosphate; Food -- Periodicals; Agriculture -- Periodicals; 664
• DOI: 10.1002/jsfa.8845
• Languages: English
• ISSNs: 0022-5142

Abstract

Abstract: BACKGROUND: Phytases are a diverse group of enzymes initiating the dephosphorylation of phytate. Phytate is considered as an anti‐nutritional compound because of its capability to chelate nutrients such as Fe 2+, Zn 2+, Mg 2+, and Ca 2+ . In this study, several bacterial isolates obtained from earthworm casts were evaluated for their phytate degrading capability. Enzymatic properties and the sequence of the corresponding phytase‐encoding gene of the selected isolate were determined. RESULTS: The phytase exhibited its highest activity at pH 4.0 and was stable from pH 3 up to pH 9. The temperature optimum was determined to be 65 °C. The strongest inhibitors of enzymatic activity were identified as vanadate, Cu 2+, and Zn 2+ . High‐performance ion chromatography analysis of enzymatic phytate dephosphorylation revealed that the first dephosphorylation product wasd/l ‐ myo ‐inositol(1, 2, 3, 4, 5)pentakisphosphate. CONCLUSION: Owing to its enzymatic properties, such as tolerance to tartrate and the presence of the consensus motifs PDTVY, GNHE, DLG, VLFH, and GHDH, this phytase could be classified as a purple acid phytase. To the best of our knowledge, this is the first report describing a bacterial purple acid phytase. © 2017 Society of Chemical Industry