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DC Field | Value | Language |
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dc.contributor.author | Alves-Prado, Heloiza Ferreira | - |
dc.contributor.author | Gomes, Eleni | - |
dc.contributor.author | da Silva, Roberto | - |
dc.date.accessioned | 2014-05-20T15:27:56Z | - |
dc.date.accessioned | 2016-10-25T18:02:54Z | - |
dc.date.available | 2014-05-20T15:27:56Z | - |
dc.date.available | 2016-10-25T18:02:54Z | - |
dc.date.issued | 2007-03-01 | - |
dc.identifier | http://dx.doi.org/10.1007/s12010-007-9038-2 | - |
dc.identifier.citation | Applied Biochemistry and Biotechnology. Totowa: Humana Press Inc., v. 137, p. 41-55, 2007. | - |
dc.identifier.issn | 0273-2289 | - |
dc.identifier.uri | http://hdl.handle.net/11449/37844 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/37844 | - |
dc.description.abstract | A cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19) from a newly isolated alkalophilic and moderately thermophilic Paenibacillus campinasensis strain H69-3 was purified as a homogeneous protein from culture supernatant. Cyclomaltodextrin glucanotransferase was produced during submerged fermentation at 45 degrees C and purified by gel filtration on Sephadex G50 ion exchange using a Q-Sepharose column and ion exchange using a Mono-Q column. The molecular weight of the purified enzyme was 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the pI was 5.3. The optimum pH for enzyme activity was 6.5, and it was stable in the pH range 6.0-11.5. The optimum temperature was 65 degrees C at pH 6.5, and it was thermally stable up to 60 degrees C without substrate during 1 h in the presence of 10 mm CaCl2. The enzyme activity increased in the presence of Co2+, Ba2+, and Mn2+. Using maltodextrin as substrate, the K-m and K-cat were 1.65 mg/mL and 347.9 mu mol/mg.min, respectively. | en |
dc.format.extent | 41-55 | - |
dc.language.iso | eng | - |
dc.publisher | Humana Press Inc | - |
dc.source | Web of Science | - |
dc.subject | CGTase characterization | pt |
dc.subject | CGTase purification | pt |
dc.subject | cyclomaltodextrin glucanotransferase | pt |
dc.subject | thermostable CGTase | pt |
dc.title | Purification and characterization of a cyclomaltodextrin glucanotransferase from Paenibacillus campinasensis strain H69-3 | en |
dc.type | outro | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.description.affiliation | UNESP, Biochem & Appl Microbiol Lab, Sao Jose do Rio Preto, SP, Brazil | - |
dc.description.affiliation | UNESP, Rio Claro, SP, Brazil | - |
dc.description.affiliationUnesp | UNESP, Biochem & Appl Microbiol Lab, Sao Jose do Rio Preto, SP, Brazil | - |
dc.description.affiliationUnesp | UNESP, Rio Claro, SP, Brazil | - |
dc.identifier.doi | 10.1007/s12010-007-9038-2 | - |
dc.identifier.wos | WOS:000246616900006 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | Applied Biochemistry and Biotechnology | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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