528-50-7Relevant articles and documents
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Deferrari,Cadenas
, p. 1070 (1963)
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Ru/P-containing porous biochar-efficiently catalyzed cascade conversion of cellulose to sorbitol in water under medium-pressure H2 atmosphere
Chen, Shuainan,Fu, Zaihui,Jiang, Dabo,Liu, Yachun,Mao, Feng,Wan, Feifei,Xiong, Manman,Yang, Long,Zhang, Chao,Zhang, Qiao
, p. 1026 - 1035 (2020/09/22)
This paper discloses a simple and productive strategy for the preparation of biochar-based bifunctional catalysts. In this strategy, very cheap bamboo powder is thermally carbonized to yield P-containing porous biochars (PBCs) by the activation of concentrated phosphoric acid (H3PO4), and the latter can be transformed into the target catalysts via loading Ru nanometer particles (NPs) on them (marked as Ru/PBCs). A series of characterizations and measurements support that PBCs have stable and rich micro-meso pores and small strong acidic protons (0.100.28 mmol￠g11) attributable to the grafted and/or skeleton phosphorus groups, as well as a strong affinity to β-1,4-glycosidic bonds, thus exhibiting a good acid catalytic activity for the hydrolysis of cellulose to glucose. More importantly, they are excellent acidic supports for the loading of Ru NPs owing to high BET surface area, which can give the loaded Ru NPs uniform and narrow distribution (16 nm). The resulting bifunctional Ru/PBCs catalysts possess excellent hydrolytic hydrogenating activity for the one-pot cascade conversion of cellulose and the optimized conditions can achieve ca. 89% hexitol yield with 98% sorbitol selectivity under relatively mild conditions. This work provides a good example for the preparation of biomass-derived bifunctional catalysts and their applications in biorefinery.
Cloning, expression and biochemical characterization of a GH1 β-glucosidase from Cellulosimicrobium cellulans
Yuan, Ye,Xu, Fenghua,Yao, Jianzhuang,Hu, Yanho,Wang, Jiao,Zhao, Tianjiao,Zhou, Yifa,Gao, Juan
, p. 362 - 371 (2017/11/03)
β-Glucosidase plays an important role in the degradation of cellulose. In this study, a novel β-glucosidase ccbgl1b gene for a glycosyl hydrolase (GH) family 1 enzyme was cloned from the genome of Cellulosimicrobium cellulans and expressed in Escherichia coli BL21 cells. The sequence contained an open reading frame of 1494 bp, encoded a polypeptide of 497 amino acid residues. The recombinant protein CcBgl1B was purified by Ni sepharose fastflow affinity chromatography and had a molecular weight of 57 kDa, as judged by SDS-PAGE. The optimum β-glucosidase activity was observed at 55 °C and pH 6.0. Recombinant CcBgl1B was found to be most active against aryl-glycosides p-nitrophenyl-β-D-glucopyranoside (pNPβGlc), followed by p-nitrophenyl-β-D-galactopyranoside (pNPβGal). Using disaccharides as substrates, the enzyme efficiently cleaved β-linked glucosyl-disaccharides, including sophorose (β-1,2-), laminaribiose (β-1,3-) and cellobiose (β-1,4-). In addition, a range of cello-oligosaccharides including cellotriose, cellotetraose and cellopentaose were hydrolysed by CcBgl1B to produce glucose. The interaction mode between the enzyme and the substrates driving the reaction was modelled using a molecular docking approach. Understanding how the GH1 enzyme CcBgl1B from C. cellulans works, particularly its activity against cello-oligosaccharides, would be potentially useful for biotechnological applications of cellulose degradation.
Hydrolysis of cellulose to glucose over carbon catalysts sulfonated via a plasma process in dilute acids
Li, Oi Lun,Ikura, Ryuhei,Ishizaki, Takahiro
, p. 4774 - 4777 (2017/10/23)
Herein, we reported a novel plasma-sulfonation process for carbon materials in dilute sulfuric acid within a few tens of minutes. The total acidic and -SO3H densities of the sulfonated carbon were 4.4 mmol g-1 and 2.2 mmol g-1, respectively. The glucose selectivity during cellulose hydrolysis using a sulfonated carbon catalyst was 83.9% and retained 98% of its performance after recycling.
