Literature DB >> 15556708

Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis.

Teresa Fontes Leal1, Isabel de Sá-Nogueira.   

Abstract

Bacillus subtilis synthesizes at least one arabinanase encoded by the abnA gene that is able to degrade the polysaccharide arabinan. Here, we report the expression in Escherichia coli of the full-length abnA coding region with a His6-tag fused to the C-terminus. The recombinant protein was secreted to the periplasmic space and correctly processed by the E. coli signal peptidase. The substrate specificity of purified AbnA, the physico-chemical properties and kinetic parameters were determined. Functional analysis studies revealed Glu 215 as a key residue for AbnA hydrolytic activity and indicated that in addition to AbnA B. subtilis secretes other enzyme(s) able to degrade linear 1,5-alpha-l-arabinan.

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Year:  2004        PMID: 15556708     DOI: 10.1016/j.femsle.2004.10.003

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  15 in total

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4.  Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus.

Authors:  Daniel Wefers; Jia Dong; Ahmed M Abdel-Hamid; Hans Müller Paul; Gabriel V Pereira; Yejun Han; Dylan Dodd; Ramiya Baskaran; Beth Mayer; Roderick I Mackie; Isaac Cann
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10.  Outer Membrane Vesicle-Mediated Codelivery of the Antifungal HSAF Metabolites and Lytic Polysaccharide Monooxygenase in the Predatory Lysobacter enzymogenes.

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