Purification and properties of phytate-specific phosphatase from Bacillus subtilis.
V K Powar,V Jagannathan +1 more
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An enzyme which liberates Pi from myo-inositol hexaphosphate (phytic acid) was shown to be present in culture filtrates of Bacillus subtilis and is the only known phytate-specific phosphatase.Abstract:
An enzyme which liberates Pi from myo-inositol hexaphosphate (phytic acid) was shown to be present in culture filtrates of Bacillus subtilis. It was purified until it was homogeneous by ultracentrifugation, but it still showed two isozymes on polyacrylamide gel electrophoresis. The enzyme differed from other previously known phytases in its metal requirement and in its specificity for phytate. It had a specific requirement for Ca2+ for its activity. The enzyme hydrolyzed only phytate and had no action on other phosphate esters tested. This B. subtilis phytase is the only known phytate-specific phosphatase. The products of hydrolysis of phytate by this enzyme were Pi and myo-inositol monophosphate. The enzyme showed optimum activity at pH 7.5. It was inhibited by Ba2+, Sr2+, Hg2+, Cd2+, and borate. Its activity was unaffected by urea, diisopropylfluorophosphate, arsenate, fluoride, mercaptoethanol, trypsin, papain, and elastase. Imagesread more
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Journal ArticleDOI
Phytases: microbial sources, production, purification, and potential biotechnological applications.
TL;DR: The review deals with phytase-producing microorganisms along with optimum conditions for its production, and various methods used for purifying phytases and their characteristics are discussed.
Journal ArticleDOI
Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis.
TL;DR: The phytase gene (phyC) was cloned from the B. subtilis VTT E-68013 genomic library and showed no homology to the sequences of other phytases nor to those of any known phosphatases, and therefore PhyC appears not to be a member of thephytase subfamily of histidine acid phosphatase but a novel enzyme having phyt enzyme activity.
Journal ArticleDOI
Molecular and catalytic properties of phytate‐degrading enzymes (phytases)
U. Konietzny,Ralf Greiner +1 more
TL;DR: The molecular features as well as catalytic properties of phytate-degrading enzymes are summarized and the physiological role of different myo-inositol phosphates is presently undergoing extensive research.
Journal ArticleDOI
Biotechnological production and applications of phytases
TL;DR: In addition to its major application in animal nutrition, phytase is also used for processing of human food and research in this field focuses on better mineral absorption and technical improvement of food processing.
Book ChapterDOI
Advances in phytase research
TL;DR: Phytase research efforts now are focused on the engineering of an improved enzyme, as increased interest in phytase as a means to reduce this phosphorus pollution is seen as an essential step to lower its cost in animal feed.
References
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