[The novel intracellular phytase of enterobacteriaceae: isolation and properties].
For the first time phytase enzyme was isolated from Pantoea vagans 3.2 strain and was subjected to investigation. The enzyme was purified about 474-fold to apparent homogeneity from the crude extract of the strain, its primary structure was determined and it was concluded that phytase of Pantoea vagans 3.2 belongs to the family of histidine acid phosphatases. It has a molecular mass of about 46 kDa and Km for the hydrolysis of sodium phytate was 0.28 mM. Some physicochemical properties ofphytase were investigated.
A D
AD
Suleĭmanova
Iu V
IuV
Danilova
R
R
Greiner
M R
MR
Sharipova
D010832:6-Phytase / Q000737:chemistry* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D004756:Enterobacteriaceae Infections / Q000201:enzymology / Q000473:pathology; D004795:Enzyme Stability; D006868:Hydrolysis; D007700:Kinetics; D008970:Molecular Weight; D020636:Pantoea / Q000201:enzymology* / Q000472:pathogenicity; D013379:Substrate Specificity; D013696:Temperature
D010832:6-Phytase