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Article: Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis

TitleMolecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis
Authors
Issue Date2002
PublisherSpringer. The Journal's web site is located at http://link.springer.de/link/service/journals/00253/index.htm
Citation
Applied Microbiology And Biotechnology, 2002, v. 59 n. 2-3, p. 190-197 How to Cite?
AbstractA novel phytase gene (phyL) was cloned from Bacillus licheniformis by multiple steps of degenerate and inverse PCR. The coding region of the phyL gene was 1,146 bp in size and a promoter region of approximately 300 bp was identified at the upstream sequence. This gene, together with a phytase gene (168phyA) identified in the B. subtilis strain 168 genome by a homology search, was cloned and over-expressed in B. subtilis using a φ105MU331 prophage vector system. Up to 35 units of phytase/ml were secreted into the culture media; and mature enzymes of around 44-47 kDa were purified for characterization. Both phytases exhibited broad temperature and pH optima and showed high thermostability. Of the two, the phytase encoded by phyL exhibited higher thermostability, even at a lower calcium concentration, as it was able to recover 80% of its original activity after denaturation at 95°C for 10 min. With their neutral pH optima and good temperature stabilities, these Bacillus phytases are good candidates for animal feed applications and transgenic studies.
Persistent Identifierhttp://hdl.handle.net/10722/84935
ISSN
2023 Impact Factor: 3.9
2023 SCImago Journal Rankings: 0.957
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTye, Aen_HK
dc.contributor.authorSiu, Fen_HK
dc.contributor.authorLeung, Ten_HK
dc.contributor.authorLim, Ben_HK
dc.date.accessioned2010-09-06T08:58:50Z-
dc.date.available2010-09-06T08:58:50Z-
dc.date.issued2002en_HK
dc.identifier.citationApplied Microbiology And Biotechnology, 2002, v. 59 n. 2-3, p. 190-197en_HK
dc.identifier.issn0175-7598en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84935-
dc.description.abstractA novel phytase gene (phyL) was cloned from Bacillus licheniformis by multiple steps of degenerate and inverse PCR. The coding region of the phyL gene was 1,146 bp in size and a promoter region of approximately 300 bp was identified at the upstream sequence. This gene, together with a phytase gene (168phyA) identified in the B. subtilis strain 168 genome by a homology search, was cloned and over-expressed in B. subtilis using a φ105MU331 prophage vector system. Up to 35 units of phytase/ml were secreted into the culture media; and mature enzymes of around 44-47 kDa were purified for characterization. Both phytases exhibited broad temperature and pH optima and showed high thermostability. Of the two, the phytase encoded by phyL exhibited higher thermostability, even at a lower calcium concentration, as it was able to recover 80% of its original activity after denaturation at 95°C for 10 min. With their neutral pH optima and good temperature stabilities, these Bacillus phytases are good candidates for animal feed applications and transgenic studies.en_HK
dc.languageengen_HK
dc.publisherSpringer. The Journal's web site is located at http://link.springer.de/link/service/journals/00253/index.htmen_HK
dc.relation.ispartofApplied Microbiology and Biotechnologyen_HK
dc.titleMolecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0175-7598&volume=59&spage=190&epage=197&date=2002&atitle=Molecular+cloning+and+the+biochemical+characterization+of+two+novel+phytases+from+B.+subtilis+168+and+B.+licheniformisen_HK
dc.identifier.emailLim, B: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLim, B=rp00744en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s00253-002-1033-5en_HK
dc.identifier.pmid12111145-
dc.identifier.scopuseid_2-s2.0-0036315591en_HK
dc.identifier.hkuros75820en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036315591&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume59en_HK
dc.identifier.issue2-3en_HK
dc.identifier.spage190en_HK
dc.identifier.epage197en_HK
dc.identifier.isiWOS:000177245900009-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridTye, A=36902988000en_HK
dc.identifier.scopusauthoridSiu, F=6701518484en_HK
dc.identifier.scopusauthoridLeung, T=16151388900en_HK
dc.identifier.scopusauthoridLim, B=7201983917en_HK
dc.identifier.issnl0175-7598-

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