NDLI: Purification and characterization of phytase from Klebsiella pneumoniae 9-3B.

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Purification and characterization of phytase from Klebsiella pneumoniae 9-3B.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Escobin-Mopera, Lotis Ohtani, Midori Sekiguchi, Sachie Sone, Teruo Abe, Ayumi Tanaka, Michiko Meevootisom, Vithaya Asano, Kozo
Description	Country affiliation: Japan Author Affiliation: Escobin-Mopera L ( Laboratory of Applied Microbiology, Graduate Faculty of Agriculture, Hokkaido University, N9 W9, Kita-ku, Sapporo, Hokkaido 060-8589, Japan.)
Abstract	Phytase, an enzyme that catalyzes the hydrolysis of phytate, was purified from Klebsiella pneumoniae 9-3B. The isolate was preferentially selected in a medium which contains phytate as a sole carbon and phosphate source. Phytic acid was utilized for growth and consequently stimulated phytase production. Phytase production was detected throughout growth and the highest phytase production was observed at the onset of stationary phase. The purification scheme including ion exchange chromatography and gel filtration resulted in a 240 and 2077 fold purification of the enzyme with 2% and 15% recovery of the total activity for liberation of inorganic phosphate and inositol, respectively. The purified phytase was a monomeric protein with an estimated molecular weight of 45kDa based on size exclusion chromatography and SDS-PAGE analyses. The phytase has an optimum pH of 4.0 and optimum temperature of 50°C. The phytase activity was slightly stimulated by Ca(2+) and EDTA and inhibited by Zn(2+) and Fe(2+). The phytase exhibited broad substrate specificity and the K(m) value for phytate was 0.04mM. The enzyme completely hydrolyzed myo-inositol hexakisphosphate (phytate) to myo-inositol and inorganic phosphate. The properties of the enzyme prove that it is a good candidate for the hydrolysis of phytate for industrial applications.
File Format	HTM / HTML
ISSN	13891723
Issue Number	5
Volume Number	113
e-ISSN	13474421
Journal	Journal of Bioscience and Bioengineering
Language	English
Publisher	Elsevier
Publisher Date	2012-05-01
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biomedical Engineering Discipline Microbiology 6-phytase Chemistry Metabolism Klebsiella Pneumoniae Enzymology Isolation & Purification Chromatography, Gel Chromatography, Ion Exchange Edetic Acid Pharmacology Electrophoresis, Polyacrylamide Gel Enzyme Activation Drug Effects Enzyme Activators Enzyme Inhibitors Hydrogen-ion Concentration Hydrolysis Metals Molecular Weight Phosphates Phytic Acid Substrate Specificity Temperature Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Bioengineering Applied Microbiology and Biotechnology Biotechnology

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