| Autor: |
dos Santos CR; Laboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais, Rua giuseppe maximo scolfaro, 10000, Campinas, SP, 13083-970, Brazil., Squina FM, Navarro AM, Oldiges DP, Paes Leme AF, Ruller R, Mort AJ, Prade R, Murakami MT |
| Jazyk: |
angličtina |
| Zdroj: |
Biotechnology letters [Biotechnol Lett] 2011 Jan; Vol. 33 (1), pp. 131-7. Date of Electronic Publication: 2010 Sep 25. |
| DOI: |
10.1007/s10529-010-0409-3 |
| Abstrakt: |
A hyperthermostable glycoside hydrolase family 51 (GH51) α-L-arabinofuranosidase from Thermotoga petrophila RKU-1 (TpAraF) was cloned, overexpressed, purified and characterized. The recombinant enzyme had optimum activity at pH 6.0 and 70°C with linear α-1,5-linked arabinoheptaose as substrate. The substrate cleavage pattern monitored by capillary zone electrophoresis showed that TpAraF is a classical exo-acting enzyme producing arabinose as its end-product. Far-UV circular dichroism analysis displayed a typical spectrum of α/β barrel proteins analogously observed for other GH51 α-L-arabinofuranosidases. Moreover, TpAraF was crystallized in two crystalline forms, which can be used to determine its crystallographic structure. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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