Structural highlights
Publication Abstract from PubMedThe 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 127U/mg. The enzyme has optimal conditions for activity at pH8.0 and 45 degrees C and its activity is only partially dependent of a bound calcium ion since 70% of the maximal activity is preserved even when 1mM 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. GH43 endo-arabinanase from Bacillus licheniformis: Structure, activity and unexpected synergistic effect on cellulose enzymatic hydrolysis.,Farro EGS, Leite AET, Silva IA, Filgueiras JG, de Azevedo ER, Polikarpov I, Nascimento AS Int J Biol Macromol. 2018 May 23;117:7-16. doi: 10.1016/j.ijbiomac.2018.05.157. PMID:29800670[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 07:36, 14 June 2018.