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Article: Properties of beta-propeller phytase expressed in transgenic tobacco

TitleProperties of beta-propeller phytase expressed in transgenic tobacco
Authors
KeywordsBacillus
Beta-propeller phytase
Phytate
Phytic acid
Tobacco
Issue Date2006
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yprep
Citation
Protein Expression And Purification, 2006, v. 46 n. 1, p. 100-106 How to Cite?
AbstractPhytases are enzymes that liberate inorganic phosphates from phytate. In a previous study, a beta-propeller phytase (168phyA) from Bacillus subtilis was introduced into transgenic tobacco, which resulted in certain phenotypic changes. In the study described herein, the recombinant phytase (t168phyA) was purified from transgenic tobacco to near homogeneity by a three-step purification scheme. The biochemical properties and kinetic parameters of t168phyA were compared with those of its counterpart from B. subtilis. t168phyA was glycosylated, and it showed a 4 kDa increase in molecular size in SDS-PAGE (44 kDa vs. 40 kDa). Although its thermostability remained unchanged, its temperature optimum shifted from 60°C to 45-50°C and its pH optimum shifted from pH 5.5 to 6.0. Kinetic data showed that the t168phyA had a lower Kcat, but a higher Km than the native enzyme. Despite these changes, t168phyA remained catalytically active and has a specific activity of 2.3 U/mg protein. These results verify the activity of recombinant Bacillus phytase that is expressed in plants. © 2005 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/54343
ISSN
2015 Impact Factor: 1.407
2015 SCImago Journal Rankings: 0.767
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, WLen_HK
dc.contributor.authorLung, SCen_HK
dc.contributor.authorLim, BLen_HK
dc.date.accessioned2009-04-03T07:43:55Z-
dc.date.available2009-04-03T07:43:55Z-
dc.date.issued2006en_HK
dc.identifier.citationProtein Expression And Purification, 2006, v. 46 n. 1, p. 100-106en_HK
dc.identifier.issn1046-5928en_HK
dc.identifier.urihttp://hdl.handle.net/10722/54343-
dc.description.abstractPhytases are enzymes that liberate inorganic phosphates from phytate. In a previous study, a beta-propeller phytase (168phyA) from Bacillus subtilis was introduced into transgenic tobacco, which resulted in certain phenotypic changes. In the study described herein, the recombinant phytase (t168phyA) was purified from transgenic tobacco to near homogeneity by a three-step purification scheme. The biochemical properties and kinetic parameters of t168phyA were compared with those of its counterpart from B. subtilis. t168phyA was glycosylated, and it showed a 4 kDa increase in molecular size in SDS-PAGE (44 kDa vs. 40 kDa). Although its thermostability remained unchanged, its temperature optimum shifted from 60°C to 45-50°C and its pH optimum shifted from pH 5.5 to 6.0. Kinetic data showed that the t168phyA had a lower Kcat, but a higher Km than the native enzyme. Despite these changes, t168phyA remained catalytically active and has a specific activity of 2.3 U/mg protein. These results verify the activity of recombinant Bacillus phytase that is expressed in plants. © 2005 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yprepen_HK
dc.relation.ispartofProtein Expression and Purificationen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectBacillusen_HK
dc.subjectBeta-propeller phytaseen_HK
dc.subjectPhytateen_HK
dc.subjectPhytic aciden_HK
dc.subjectTobaccoen_HK
dc.subject.mesh6-Phytase - genetics - isolation & purification - metabolismen_HK
dc.subject.meshBacillus subtilis - enzymologyen_HK
dc.subject.meshBacterial Proteins - genetics - metabolismen_HK
dc.subject.meshHydrogen-Ion Concentrationen_HK
dc.subject.meshTobacco - enzymology - geneticsen_HK
dc.titleProperties of beta-propeller phytase expressed in transgenic tobaccoen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1046-5928&volume=46&issue=1&spage=100&epage=106&date=2005&atitle=Properties+of+beta-propeller+phytase+expressed+in+transgenic+tobaccoen_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.pep.2005.07.019en_HK
dc.identifier.pmid16137892-
dc.identifier.scopuseid_2-s2.0-32644465044en_HK
dc.identifier.hkuros103171-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-32644465044&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume46en_HK
dc.identifier.issue1en_HK
dc.identifier.spage100en_HK
dc.identifier.epage106en_HK
dc.identifier.isiWOS:000235902700012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, WL=8619522000en_HK
dc.identifier.scopusauthoridLung, SC=8619522500en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK

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