Two polypeptides showing α-l-arabinofuranosidase activity have been purified to homogeneity from culture supernatants of a Bacillus subtilis clone harbouring the xynD gene [Gosalbes et al. (1991) J Bacteriol 173: 7705–7710] from Bacillus polymyxa. Both polypeptides, with determined molecular masses of 64 kDa and 53 kDa, share the same sequence at their N termini, which also coincides with the sequence deduced for the mature protein from the previously determined sequence of nucleotides (Gosalbes et al. 1991). The two polypeptides have been biochemically characterized. Arabinose is the unique product released from arabinose-containing xylans which are substrates for both enzyme forms. Other natural arabinose-containing polysaccharides, such as arabinogalactans, are not attacked by them but some artificial arabinose derivatives are good substrates for both polypeptides. Their arabinose-releasing activity on arabinoxylans facilitates the hydrolysis of the xylan backbone by some endoxylanases from Bacillus polymyxa.
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Departmento de Biotechnología, Instituto de Agroquímica y Tecnología de los Alimentos, Consejo Superior de Investigaciones Científicas, Apartado de Correos n° 73, 46080, Burjassot, Valencia, Spain
P. Morales, J. M. Sendra & J. A. Pérez-González
Morales, P., Sendra, J.M. & Pérez-González, J.A. Purification and characterization of an arabinofuranosidase from Bacillus polymyxa expressed in Bacillus subtilis . Appl Microbiol Biotechnol 44, 112–117 (1995). https://doi.org/10.1007/BF00164489
Received: 19 December 1994
Revised: 14 March 1995
Accepted: 03 April 1995
Issue Date: December 1995
DOI: https://doi.org/10.1007/BF00164489
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