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PDBsum entry 6b7k
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References listed in PDB file
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Key reference
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Title
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Gh43 endo-Arabinanase from bacillus licheniformis: structure, Activity and unexpected synergistic effect on cellulose enzymatic hydrolysis.
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Authors
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E.G.S.Farro,
A.E.T.Leite,
I.A.Silva,
J.G.Filgueiras,
E.R.De azevedo,
I.Polikarpov,
A.S.Nascimento.
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Ref.
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Int J Biol Macromol, 2018,
117,
7.
[DOI no: ]
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PubMed id
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Abstract
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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.
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