Xylobiose (6CI,7CI,8CI)/Xylobiose/D-Xylose, 4-O-β-D-xylopyranosyl- (9CI)/1,4-β-Xylobiose/4-O-β-D-Xylopyranosyl-D-xylose/D-Xylose, 4-O-β-D-xylopyranosyl-
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The production of high-purity xylobiose from lignocellulose is an expensive and tedious process. In this work, the production of xylobiose from enzymatic hydrolysis of alkaline oxidation pretreated sugarcane bagasse was investigated. Furthermore, a simple process for the separation of xylobiose from enzymatic hydrolysate by activated carbon absorption, water washing, and ethanol-water desorption was developed. Under the optimized separation conditions, 96.77% xylobiose was adsorbed at 16% activated carbon loadings. Moreover, xylose and acetate could not be detected after washing by 3-fold volume of water. Xylobiose with 80.16% yield was eluted by 5-fold volume of 5% (v/v) ethanol-water. The reusability of activated carbon was evaluated by 5 cycles of adsorption-desorption process, suggesting that the activated carbon exhibited good reusability. The separated xylobiose sample with high-purity (97.29%) was confirmed by HPLC, ESI-MS, and NMR. Overall, this study provided a low-cost and robust technology for the production and separation of high-purity xylobiose from lignocellulose.
Copyright © 2019 Elsevier Ltd. All rights reserved.
Activated carbon adsorption; Ethanol-water desorption; High-purity xylobiose; Separation
Production, separation, and characterization of high-purity xylobiose from enzymatic hydrolysis of alkaline oxidation pretreated sugarcane bagasse.
Li H1, Chen X2, Xiong L1, Zhang L2, Chen X1, Wang C1, Huang C1, Chen X3.
Fungal endo-β-1,4-xylanases (endo-xylanases) can hydrolyze xylan into xylooligosaccharides (XOS), and have potential biotechnological applications for the exploitation of natural renewable polysaccharides. In the current study, we aimed to screen and characterize an efficient fungal endo-xylanase from 100 natural humus-rich soil samples collected in Guizhou Province, China, using extracted sugarcane bagasse xylan (SBX) as the sole carbon source. Initially, 182 fungal isolates producing xylanases were selected, among which Trichoderma sp. strain TP3-36 was identified as showing the highest xylanase activity of 295 U/mL with xylobiose (X2) as the main product when beechwood xylan was used as substrate. Subsequently, a glycoside hydrolase family 11 endo-xylanase, TXyn11A, was purified from strain TP3-36, and its optimal pH and temperature for activity against beechwood xylan were identified to be 5.0 and 55 °C, respectively. TXyn11A was stable across a broad pH range (3.0-10.0), and exhibited strict substrate specificity, including xylan from beechwood, wheat, rye, and sugarcane bagasse, with Km and Vmax values of 5 mg/mL and 1250 μmol/mg min, respectively, toward beechwood xylan. Intriguingly, the main product obtained from hydrolysis of beechwood xylan by TXyn11A was xylobiose, whereas SBX hydrolysis resulted in both X2 and xylotriose. Overall, these characteristics of the endo-xylanase TXyn11A indicate several potential industrial applications.
Endo-xylanase; Sugarcane bagasse xylanase; Trichoderma sp.; Xylobiose
Purification and characterization of an endo-xylanase from Trichoderma sp., with xylobiose as the main product from xylan hydrolysis.
Fu LH1, Jiang N1, Li CX1, Luo XM1, Zhao S2, Feng JX3.
2019 Oct 31
Biotechnologies that aim to produce renewable fuels, chemicals, and bioproducts from residual ligno(hemi)cellulosic biomass mostly rely on enzymatic depolymerization of plant cell walls (PCW). This process requires an arsenal of diverse enzymes, including xylanases, which synergistically act on the hemicellulose, reducing the long and complex xylan chains to oligomers and simple sugars. Thus, xylanases play a crucial role in PCW depolymerization. Until recently, the largest xylanase family, glycoside hydrolase family 11 (GH11) has been exclusively represented by endo-catalytic β-1,4- and β-1,3-xylanases. Analysis of a metatranscriptome library from a microbial lignocellulose community resulted in the identification of an unusual exo-acting GH11 β-1,4-xylanase (MetXyn11). Detailed characterization has been performed on recombinant MetXyn11 including determination of its low-resolution small-angle X-ray scattering (SAXS) molecular envelope in solution. Our results reveal that MetXyn11 is a monomeric globular enzyme that liberates xylobiose from heteroxylans as the only product. MetXyn11 has an optimal activity in a pH range from 6 to 9 and an optimal temperature of 50 °C. The enzyme maintained above 65% of its original activity in the pH range 5 to 6 after being incubated for 72 h at 50 °C. Addition of the enzyme to a commercial enzymatic cocktail (CelicCtec3) promoted a significant increase of enzymatic hydrolysis yields of hydrothermally pretreated sugarcane bagasse (16% after 24 h of hydrolysis).
Biochemical characterization; GH11 exo-β-1,4-xylanase; Metatranscriptome; Small-Angle X-ray scattering; Synergism
Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium.
Evangelista DE1, de Oliveira Arnoldi Pellegrini V1, Santo ME1, McQueen-Mason S2, Bruce NC2, Polikarpov I3.