552-71-6Relevant articles and documents
Hydrolysis behaviors of sugarcane bagasse pith in subcritical carbon dioxide-water
Liang, Jiezhen,Chen, Xiaopeng,Wang, Linlin,Wei, Xiaojie,Qiu, Feifei,Lu, Chaochao
, p. 99322 - 99330 (2016/11/02)
The aim of this study was to describe the hydrolysis behavior of sugarcane bagasse pith (SCBP) in subcritical CO2-water. The hydrolysis was carried out in a batch reactor using different temperatures (160 to 260 °C), liquid to solid ratios (20:1 to 100:1), CO2 pressures (0 to 7.3 MPa), stirring speeds (0 to 500 rpm) and reaction times (0 to 40 min). The highest total reducing sugar yield (43.6%) was obtained at 200 °C, liquid to solid ratio 30:1, 2 MPa CO2, 500 rpm and 50 min. Two-dimensional heteronuclear single quantum coherence (2D HSQC) nuclear magnetic resonance (NMR), scanning electron microscopy (SEM) and Fourier transform infrared spectrometry (FT-IR) were used to help elucidate the physical and chemical characteristics of the raw material and residual solid particles, with results consistent with the removal of hemicellulose during hydrolysis. The changes in the concentration of products with time were analyzed to understand product distribution through high-performance liquid chromatography (HPLC) and to infer the reaction mechanism.
The enhancement of xylose monomer and xylotriose degradation by inorganic salts in aqueous solutions at 180 °C
Liu, Chaogang,Wyman, Charles E.
, p. 2550 - 2556 (2007/10/03)
The inorganic salts KCl, NaCl, CaCl2, MgCl2, and FeCl3, and especially the latter, significantly increased xylose monomer and xylotriose degradation in water heated to 180 °C with unaccountable losses of xylose amounting to as high as 65% and 78% for xylose and xylotriose, respectively, after 20 min incubation with 0.8% FeCl3. Furthermore, losses of both xylose and xylotriose were well described by first order homogeneous kinetics, and the rate constants for xylose and xylotriose disappearance increased 6- and 49-fold, respectively, when treated with 0.8% FeCl3 solution compared to treatment with just pressurized hot water at the same temperature. Although the addition of these inorganic salts produced a significant drop in pH, the degradation rates with salts were much faster than could be accounted for by a pH change. For example, the rate constants for the disappearance of xylose and xylotriose with 0.8% FeCl3 were 3-fold and 7-fold greater, respectively, than for treatment with very dilute sulfuric acid at the same pH. In addition, xylose losses were greater than could be accounted for by just furfural production, suggesting that other degradation products were also formed, and xylose losses to unidentified compounds increased significantly with the addition of FeCl3. The unidentified compounds could be formed through aqueous furfural resinification and condensation reactions that are accelerated by FeCl3, but the actual mechanisms are still not clear.
Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile
Katapodis, Petros,Vrsanska, Maria,Kekos, Dimitris,Nerinckx, Wim,Biely, Peter,Claeyssens, Marc,Macris, Basil J.,Christakopoulos, Paul
, p. 1881 - 1890 (2007/10/03)
An endo-β-1,4-xylanase (1,4-β-D-xylan xylanoxydrolase, EC 3.2.1.8) present in culture filtrates of Sporotrichum thermophile ATCC 34628 was purified to homogeneity by Q-Sepharose and Sephacryl S-200 column chromatographies. The enzyme has a molecular mass of 25,000 Da, an isoelectric point of 6.7, and is optimally active at pH 5 and at 70°C. Thin-layer chromatography (TLC) analysis showed that endo-xylanase liberates mainly xylose (Xyl) and xylobiose (Xyl2) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methylglucuronoxylan and rhodymenan (a β-(1→4)-β(1→3)-xylan). Also, the enzyme releases an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. Analysis of reaction mixtures by high performance liquid chromatography (HPLC) revealed that the enzyme cleaves preferentially the internal glycosidic bonds of xylooligosaccharides, [1-3H]-xylooligosaccharides and xylan. The enzyme also hydrolyses the 4-methylumbelliferyl glycosides of β-xylobiose and β-xylotriose at the second glycosidic bond adjacent to the aglycon. The endoxylanase is not active on pNPX and pNPC. The enzyme mediates a decrease in the viscosity of xylan associated with a release of only small amounts of reducing sugar. The enzyme is irreversibly inhibited by series of ω-epoxyalkyl glycosides of D-xylopyranose. The results suggest that the endoxylanase from S. thermophile has catalytic properties similar to the enzymes belonging to family 11.
