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Article: Hydrolysis of precipitated phytate by three distinct families of phytases

TitleHydrolysis of precipitated phytate by three distinct families of phytases
Authors
KeywordsBeta-propeller phytase
Citrate
Histidine acid phosphatase
Malate
Oxalate
Phytate
Purple acid phosphatase
Issue Date2006
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/soilbio
Citation
Soil Biology And Biochemistry, 2006, v. 38 n. 6, p. 1316-1324 How to Cite?
AbstractWhile genetically modified plants that secrete histidine acid phosphatases (HAPs), β-propeller phytases (BPPs) and purple acid phosphatases (PAPs) have been shown to assimilate soluble phytate, little is known about whether these plants have the ability to hydrolyze precipitated phytate. In this study, the ability of representative members of these three classes of phytases to hydrolyze metal-phytate salts and to hydrolyze phytate adsorbed to aluminum precipitates was compared. All three phytases were able to hydrolyze Ca 2+-, Mg 2+-, and Mn 2+-phytates, but were unable to hydrolyze Al 3+-, Fe 2+-, Fe 3+-, Cu 2+-, and Zn 2+-phytates. When these ions were present, the hydrolysis of Ca 2+-phytate was prevented. Citrate was more potent than malate and oxalate in solubilizing some of these phytate salts for enzyme hydrolysis. Phytate adsorbed to aluminum precipitates was resistant to all three enzymes, except when organic acids were added (citrate>oxalate>malate). While increasing concentrations of organic acids were inhibitory to enzyme activity (oxalate >citrate>malate), PAP was more resistant to citrate than HAP. As desorption of phytate from a solid surface by organic acids is essential for phytase activity, the genetic engineering of plants that enhances the secretion of both citrate and phytases from the root may be a feasible approach to improving soil phytate assimilation. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/54342
ISSN
2015 Impact Factor: 4.152
2015 SCImago Journal Rankings: 2.382
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, Jen_HK
dc.contributor.authorLeung, Aen_HK
dc.contributor.authorLeung, Cen_HK
dc.contributor.authorLim, BLen_HK
dc.date.accessioned2009-04-03T07:43:54Z-
dc.date.available2009-04-03T07:43:54Z-
dc.date.issued2006en_HK
dc.identifier.citationSoil Biology And Biochemistry, 2006, v. 38 n. 6, p. 1316-1324en_HK
dc.identifier.issn0038-0717en_HK
dc.identifier.urihttp://hdl.handle.net/10722/54342-
dc.description.abstractWhile genetically modified plants that secrete histidine acid phosphatases (HAPs), β-propeller phytases (BPPs) and purple acid phosphatases (PAPs) have been shown to assimilate soluble phytate, little is known about whether these plants have the ability to hydrolyze precipitated phytate. In this study, the ability of representative members of these three classes of phytases to hydrolyze metal-phytate salts and to hydrolyze phytate adsorbed to aluminum precipitates was compared. All three phytases were able to hydrolyze Ca 2+-, Mg 2+-, and Mn 2+-phytates, but were unable to hydrolyze Al 3+-, Fe 2+-, Fe 3+-, Cu 2+-, and Zn 2+-phytates. When these ions were present, the hydrolysis of Ca 2+-phytate was prevented. Citrate was more potent than malate and oxalate in solubilizing some of these phytate salts for enzyme hydrolysis. Phytate adsorbed to aluminum precipitates was resistant to all three enzymes, except when organic acids were added (citrate>oxalate>malate). While increasing concentrations of organic acids were inhibitory to enzyme activity (oxalate >citrate>malate), PAP was more resistant to citrate than HAP. As desorption of phytate from a solid surface by organic acids is essential for phytase activity, the genetic engineering of plants that enhances the secretion of both citrate and phytases from the root may be a feasible approach to improving soil phytate assimilation. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/soilbioen_HK
dc.relation.ispartofSoil Biology and Biochemistryen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectBeta-propeller phytaseen_HK
dc.subjectCitrateen_HK
dc.subjectHistidine acid phosphataseen_HK
dc.subjectMalateen_HK
dc.subjectOxalateen_HK
dc.subjectPhytateen_HK
dc.subjectPurple acid phosphataseen_HK
dc.titleHydrolysis of precipitated phytate by three distinct families of phytasesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0038-0717&volume=38&issue=6&spage=1316&epage=1324&date=2006&atitle=Hydrolysis+of+precipitated+phytate+by+three+distinct+families+of+phytasesen_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1016/j.soilbio.2005.08.021en_HK
dc.identifier.scopuseid_2-s2.0-33646252921en_HK
dc.identifier.hkuros116646-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646252921&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume38en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1316en_HK
dc.identifier.epage1324en_HK
dc.identifier.isiWOS:000238028700018-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridTang, J=23393649200en_HK
dc.identifier.scopusauthoridLeung, A=7403012653en_HK
dc.identifier.scopusauthoridLeung, C=13204640800en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK

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