7643-75-6Relevant articles and documents
Action patterns and mapping of the substrate-binding regions of endo-(1 → 5)-α-L-arabinanases from Aspergillus niger and Aspergillus aculeatus
Pitson, Stuart M.,Voragen, Alphons G.J.,Vincken, Jean-Paul,Beldman, Gerrit
, p. 207 - 218 (1997)
The substrate binding sites of endo-(1 → 5)-α-L-arabinanases (EC 3.2.1.99) from Aspergillus niger and Aspergillus aculeatus were investigated using reduced and regular (1 → 5)-α-L-arabino-oligosaccharides and high performance anion exchange chromatographic analysis. Calculation of bond cleavage frequencies and k(cat)/K(m), parameters for these substrates enabled the determination of the number of arabinofuranosyl binding subsites and the estimation of the binding affinities of each subsite. The A. aculeatus endo-arabinanase has six subsites arranged symmetrically around the catalytic site, while the A. niger endo-arabinanase has five subsites; two from the catalytic site towards the non-reducing end of the bound substrate and three toward the reducing end. The two subsites directly adjacent to the catalytic sites in both the A. niger and A. aculeatus endo-arabinanase have near-zero net free energy of binding. These results are unlike most glycopyranosyl endo-hydrolases studied which have net negative (unfavourable) energies of interaction at these two subsites, and may be related to the greater conformational flexibility of arabinofuranosyl residues than glycopyranosyl residues. The complete subsite maps are also rationalized with regard to the observed action patterns of these enzymes on linear (1 → 5)-α-L-arabinan.
Hydrogenolysis of sorbitol into valuable C3-C2 alcohols at low H2 pressure promoted by the heterogeneous Pd/Fe3O4 catalyst
Gumina, Bianca,Mauriello, Francesco,Pietropaolo, Rosario,Galvagno, Signorino,Espro, Claudia
, p. 152 - 160 (2018/02/17)
The hydrogenolysis of sorbitol and various C5-C3 polyols (xylitol; erythritol; 1,2- 1,4- and 2,3-butandiol; 1,2-propandiol; glycerol) have been investigated at low molecular hydrogen pressure (5 bar) by using Pd/Fe3O4, as heterogeneous catalyst and water as the reaction medium. Catalytic experiments show that the carbon chain of polyols is initially shortened through dehydrogenation/decarbonylation and dehydrogenation/retro-aldol mechanisms followed by a series of cascade reactions that include dehydrogenation/decarbonylation and dehydration/hydrogenation processes. At 240 °C, sorbitol is fully converted into lower alcohols with ethanol being the main reaction product in liquid phase.
Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates
Jones, Darryl R.,Uddin, Muhammed Salah,Gruninger, Robert J.,Pham, Thi Thanh My,Thomas, Dallas,Boraston, Alisdair B.,Briggs, Jonathan,Pluvinage, Benjamin,McAllister, Tim A.,Forster, Robert J.,Tsang, Adrian,Selinger, L. Brent,Abbott, D. Wade
, p. 12606 - 12620 (2017/08/02)
Enzyme activities that improve digestion of recalcitrant plant cell wall polysaccharides may offer solutions for sustainable industries. To this end, anaerobic fungi in the rumen have been identified as a promising source of novel carbohydrate active enzymes (CAZymes) that modify plant cell wall polysaccharides and other complex glycans. Many CAZymes share insufficient sequence identity to characterized proteins from other microbial ecosystems to infer their function; thus presenting challenges to their identification. In this study, four rumen fungal genes (nf2152, nf2215, nf2523, and pr2455) were identified that encode family 39 glycoside hydrolases (GH39s), and have conserved structural features with GH51s. Two recombinant proteins, NF2152 and NF2523, were characterized using a variety of biochemical and structural techniques, and were determined to have distinct catalytic activities. NF2152 releases a single product, β1,2-arabinobiose (Ara2) from sugar beet arabinan (SBA), and β1,2-Ara2 and α-1,2-galactoarabinose (Gal-Ara) from rye arabinoxylan (RAX). NF2523 exclusively releases α-1,2-Gal-Ara from RAX, which represents the first description of a galacto-(-1,2)-arabinosidase. Both β-1,2-Ara2 and α-1,2-Gal-Ara are disaccharides not previously described within SBA and RAX. In this regard, the enzymes studied here may represent valuable new biocatalytic tools for investigating the structures of rare arabinosyl-containing glycans, and potentially for facilitating their modification in industrial applications.
