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Article: Stabilization of beta-propeller phytase by introducing Xaa→Pro and Gly→Ala substitutions at consensus positions

TitleStabilization of beta-propeller phytase by introducing Xaa→Pro and Gly→Ala substitutions at consensus positions
Authors
KeywordsBeta-propeller phytase
Proline
Protein engineering
Protein stability
Unfolding entropy
Issue Date2008
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htm
Citation
Protein And Peptide Letters, 2008, v. 15 n. 3, p. 297-299 How to Cite?
AbstractPhytases play important roles in agricultural and feed industries. In this study, the stability of a beta-propeller phytase, PhyL, from Bacillus licheniformis was successfully improved by introducing Xaa→Pro and Gly→Ala substitutions at consensus positions. Our results suggest that Gly→Ala substitution is a more promising strategy to improve protein stability. © 2008 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/89195
ISSN
2021 Impact Factor: 1.927
2020 SCImago Journal Rankings: 0.432
References

 

DC FieldValueLanguage
dc.contributor.authorTung, ETKen_HK
dc.contributor.authorMa, HWen_HK
dc.contributor.authorCheng, Cen_HK
dc.contributor.authorLim, BLen_HK
dc.contributor.authorWong, KBen_HK
dc.date.accessioned2010-09-06T09:53:43Z-
dc.date.available2010-09-06T09:53:43Z-
dc.date.issued2008en_HK
dc.identifier.citationProtein And Peptide Letters, 2008, v. 15 n. 3, p. 297-299en_HK
dc.identifier.issn0929-8665en_HK
dc.identifier.urihttp://hdl.handle.net/10722/89195-
dc.description.abstractPhytases play important roles in agricultural and feed industries. In this study, the stability of a beta-propeller phytase, PhyL, from Bacillus licheniformis was successfully improved by introducing Xaa→Pro and Gly→Ala substitutions at consensus positions. Our results suggest that Gly→Ala substitution is a more promising strategy to improve protein stability. © 2008 Bentham Science Publishers Ltd.en_HK
dc.languageengen_HK
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/ppl/index.htmen_HK
dc.relation.ispartofProtein and Peptide Lettersen_HK
dc.subjectBeta-propeller phytase-
dc.subjectProline-
dc.subjectProtein engineering-
dc.subjectProtein stability-
dc.subjectUnfolding entropy-
dc.subject.mesh6-Phytase - chemistryen_HK
dc.subject.meshAlanine - chemistryen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAmino Acid Substitutionen_HK
dc.subject.meshBacillus - enzymologyen_HK
dc.subject.meshConsensus Sequenceen_HK
dc.subject.meshGlycine - chemistryen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshProline - chemistryen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshSequence Alignmenten_HK
dc.titleStabilization of beta-propeller phytase by introducing Xaa→Pro and Gly→Ala substitutions at consensus positionsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0929-8665&volume=15&spage=297&epage=299&date=2008&atitle=Stabilization+of+beta-propeller+phytase+by+introducing+Xaa→Pro+and+Gly→Ala+substitutions+at+consensus+positions.+en_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.2174/092986608783744216en_HK
dc.identifier.pmid18336361-
dc.identifier.scopuseid_2-s2.0-41449091341en_HK
dc.identifier.hkuros149505en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-41449091341&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume15en_HK
dc.identifier.issue3en_HK
dc.identifier.spage297en_HK
dc.identifier.epage299en_HK
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridTung, ETK=23398349800en_HK
dc.identifier.scopusauthoridMa, HW=23988907100en_HK
dc.identifier.scopusauthoridCheng, C=7404797223en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK
dc.identifier.scopusauthoridWong, KB=7404759301en_HK
dc.identifier.citeulike2465545-
dc.identifier.issnl0929-8665-

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