Abstract:
:The hydrolysis of the plant biomass provides many interesting opportunities for the generation of building blocks for the green chemistry industrial applications. An important progress has been made for the hydrolysis of the cellulosic component of the biomass while, for the hemicellulosic components, the advances are less straightforward. Here, we describe the cloning, expression and biochemical and structural characterization of BlAbn1, a GH43 arabinanase from Bacillus licheniformis. This enzyme is selective for linear arabinan and efficiently hydrolyzes this substrate, with a specific activity of 127 U/mg. The enzyme has optimal conditions for activity at pH 8.0 and 45 °C and its activity is only partially dependent of a bound calcium ion since 70% of the maximal activity is preserved even when 1 mM EDTA is added to the reaction medium. BlAbn1 crystal structure revealed a typical GH43 fold and narrow active site, which explains the selectivity for linear substrates. Unexpectedly, the enzyme showed a synergic effect with the commercial cocktail Accellerase 1500 on cellulose hydrolysis. Scanning Electron Microscopy, Solid-State NMR and relaxometry data indicate that the enzyme weakens the interaction between cellulose fibers in filter paper, thus providing an increased access to the cellulases of the cocktail.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Farro EGS,Leite AET,Silva IA,Filgueiras JG,de Azevedo ER,Polikarpov I,Nascimento ASdoi
10.1016/j.ijbiomac.2018.05.157subject
Has Abstractpub_date
2018-10-01 00:00:00pages
7-16eissn
0141-8130issn
1879-0003pii
S0141-8130(18)30401-Xjournal_volume
117pub_type
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