Phytase: Difference between revisions
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[[Image:Phytate.png|thumb|[[Phytate]]]] |
[[Image:Phytate.png|thumb|[[Phytate]]]] |
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'''Phytase''' (myo-inositol hexakisphosphate phosphohydrolase) are a type of [[phosphatase]] enzyme that catalyzes the hydrolysis of [[phytic acid]] (myo-inositol hexakisphosphate), an undigestable, organic form of [[phosphorus]] that is found in [[grain]]s and [[oil seeds]], and releases a useable form of inorganic [[phosphorus]].<ref name="Mullaney1">{{cite journal |author= Mullaney EJ, Daly CB, Ullah AH |year=2000 |title= Advances in phytase research |journal= Adv Appl Microbiol |volume=47 |pages=157-199 |pmid=12876797}}</ref> While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been the most commonly detected and characterized from fungi.<ref name="Mullaney2">{{cite journal |author= Mullaney EJ, Ullah AH |year=2003 |title= The term phytase comprises several different classes of enzymes |journal= Biochem Biophys Res Commun |volume=312 |issue=1 |pages=179-184 |pmid=14630039}}</ref> Four distinct classes of phytase have been characterized in the literature: histidine acid phosphatases (HAPS), B-propeller phytases, purple acid phosphatases,<ref name=Mullaney2/> and most recently, [[protein tyrosine phosphatase]]-like phytases (PTP-like phytases).<ref name="Puhl1">{{cite journal |author= Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB |year=2007 |title= Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase |journal= Protein Science |volume=16 |issue=7 |pages=1368-1378 |pmid=17567745}}</ref> |
'''Phytase''' (myo-inositol hexakisphosphate phosphohydrolase) are a type of [[phosphatase]] enzyme that catalyzes the hydrolysis of [[phytic acid]] (myo-inositol hexakisphosphate), an undigestable, organic form of [[phosphorus]] that is found in [[grain]]s and [[oil seeds]], and releases a useable form of inorganic [[phosphorus]].<ref name="Mullaney1">{{cite journal |author= Mullaney EJ, Daly CB, Ullah AH |year=2000 |title= Advances in phytase research |journal= Adv Appl Microbiol |volume=47 |pages=157-199 |pmid=12876797}}</ref> While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been the most commonly detected and characterized from fungi.<ref name="Mullaney2">{{cite journal |author= Mullaney EJ, Ullah AH |year=2003 |title= The term phytase comprises several different classes of enzymes |journal= Biochem Biophys Res Commun |volume=312 |issue=1 |pages=179-184 |pmid=14630039}}</ref> Four distinct classes of phytase have been characterized in the literature: histidine acid phosphatases (HAPS), B-propeller phytases, purple acid phosphatases,<ref name=Mullaney2/> and most recently, [[protein tyrosine phosphatase]]-like phytases (PTP-like phytases).<ref name="Puhl1">{{cite journal |author= Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB |year=2007 |title= Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase |journal= Protein Science |volume=16 |issue=7 |pages=1368-1378 |pmid=17567745}}</ref> Most phytases show a broad substrate specificity, having the ability to hydrolyze many phosphorylated compounds that are not structurally similar to phytic acid such as [[ADP]], [[ATP]], phenyl phosphate, [[fructose 1,6-bisphosphate]], [[glucose 6-phosphate]], [[glycerophosphate]] and [[3-phosphoglycerate]].<ref name="Konietzny1">{{cite journal |author= Konietzny U, Greiner R |year=2002 |title= Molecular and catalytic properties of phytate-degrading enzymes (phytases) |journal= Int J Food Sci Technol |volume=37 |pages=791-812 |DOI=10.1046/j.1365-2621.2002.00617.x}}</ref> Only a few phytases have been described as highly specific for phytic acid, such as phytases from ''[[Bacillus]] sp.'', ''[[Aspergillus]] sp.'', [[E. coli]]<ref name=Konietzny1/> and those phytases belonging to the class of PTP-like phytases<ref name="Puhl2">{{cite journal |author= Puhl AA, Greiner R, Selinger LB |year=2009 |title= Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii |journal= Appl Microbiol Biotechnol |volume=82 |issue=1 |pages=95-103 |pmid=18853154}}</ref> |
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Phytase is normally produced (endogenous phytase) in [[ruminants]].<ref>http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T6R-47P91J1-7-3&_cdi=5037&_user=525220&_pii=S030881460200417X&_orig=search&_coverDate=05%2F31%2F2003&_sk=999189997&view=c&wchp=dGLzVlb-zSkWA&md5=49dfcd00d7e0dad37bb86813ebd14a36&ie=/sdarticle.pdf</ref>. Non-ruminants ([[monogastric]] animals) like human beings, dogs, birds, etc. do not produce this enzyme. Research in the field of animal nutrition has put forth the idea of supplementing phytase enzyme, exogenously, so as to make available bound nutrients like [[calcium]], [[phosphorus]], other minerals, [[carbohydrates]] and [[proteins]]. |
Phytase is normally produced (endogenous phytase) in [[ruminants]].<ref>http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T6R-47P91J1-7-3&_cdi=5037&_user=525220&_pii=S030881460200417X&_orig=search&_coverDate=05%2F31%2F2003&_sk=999189997&view=c&wchp=dGLzVlb-zSkWA&md5=49dfcd00d7e0dad37bb86813ebd14a36&ie=/sdarticle.pdf</ref>. Non-ruminants ([[monogastric]] animals) like human beings, dogs, birds, etc. do not produce this enzyme. Research in the field of animal nutrition has put forth the idea of supplementing phytase enzyme, exogenously, so as to make available bound nutrients like [[calcium]], [[phosphorus]], other minerals, [[carbohydrates]] and [[proteins]]. |
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Revision as of 16:53, 9 January 2011
Phytase (myo-inositol hexakisphosphate phosphohydrolase) are a type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate), an undigestable, organic form of phosphorus that is found in grains and oil seeds, and releases a useable form of inorganic phosphorus.[1] While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been the most commonly detected and characterized from fungi.[2] Four distinct classes of phytase have been characterized in the literature: histidine acid phosphatases (HAPS), B-propeller phytases, purple acid phosphatases,[2] and most recently, protein tyrosine phosphatase-like phytases (PTP-like phytases).[3] Most phytases show a broad substrate specificity, having the ability to hydrolyze many phosphorylated compounds that are not structurally similar to phytic acid such as ADP, ATP, phenyl phosphate, fructose 1,6-bisphosphate, glucose 6-phosphate, glycerophosphate and 3-phosphoglycerate.[4] Only a few phytases have been described as highly specific for phytic acid, such as phytases from Bacillus sp., Aspergillus sp., E. coli[4] and those phytases belonging to the class of PTP-like phytases[5]
Phytase is normally produced (endogenous phytase) in ruminants.[6]. Non-ruminants (monogastric animals) like human beings, dogs, birds, etc. do not produce this enzyme. Research in the field of animal nutrition has put forth the idea of supplementing phytase enzyme, exogenously, so as to make available bound nutrients like calcium, phosphorus, other minerals, carbohydrates and proteins.
Phytase is used as an animal feed supplement - often in poultry and swine - to enhance the nutritive value of plant material by liberation of inorganic phosphate from phytic acid (myo-inositol hexakisphosphate). Phytase can be purified from transgenic microbes and has been produced recently in transgenic canola, alfalfa and rice plants. Phytase can also be produced on a large scale through cellulosic biomass fermentation using genetically modified (GM) yeast. Phytase can also be isolated from basidiomycetes fungi. A strain of transgenic pig can produce phytase, thus reducing their environmental impact.
It is classified under EC 3.1.3.26.[7]
References
- ^ Mullaney EJ, Daly CB, Ullah AH (2000). "Advances in phytase research". Adv Appl Microbiol. 47: 157–199. PMID 12876797.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b Mullaney EJ, Ullah AH (2003). "The term phytase comprises several different classes of enzymes". Biochem Biophys Res Commun. 312 (1): 179–184. PMID 14630039.
- ^ Puhl AA, Gruninger RJ, Greiner R, Janzen TW, Mosimann SC, Selinger LB (2007). "Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase". Protein Science. 16 (7): 1368–1378. PMID 17567745.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b Konietzny U, Greiner R (2002). "Molecular and catalytic properties of phytate-degrading enzymes (phytases)". Int J Food Sci Technol. 37: 791–812. doi:10.1046/j.1365-2621.2002.00617.x.
- ^ Puhl AA, Greiner R, Selinger LB (2009). "Stereospecificity of myo-inositol hexakisphosphate hydrolysis by a protein tyrosine phosphatase-like inositol polyphosphatase from Megasphaera elsdenii". Appl Microbiol Biotechnol. 82 (1): 95–103. PMID 18853154.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T6R-47P91J1-7-3&_cdi=5037&_user=525220&_pii=S030881460200417X&_orig=search&_coverDate=05%2F31%2F2003&_sk=999189997&view=c&wchp=dGLzVlb-zSkWA&md5=49dfcd00d7e0dad37bb86813ebd14a36&ie=/sdarticle.pdf
- ^ Phytase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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