Characterisation of lignin-carbohydrate complexes (LCCs) of spruce wood (Picea abies L.) isolated with two methods

Holzforschung ◽  
2006 ◽  
Vol 60 (2) ◽  
pp. 156-161 ◽  
Author(s):  
Martin Lawoko ◽  
Gunnar Henriksson ◽  
Göran Gellerstedt

Abstract A method for the quantitative isolation of lignin-carbohydrate complexes (LCCs) in a softwood is presented. The isolation steps involve partial enzymatic hydrolysis of cellulose, subsequent swelling in urea, and quantitative dissolution into four major fractions: (1) a galactoglucomannan LCC containing ∼8% of the wood lignin; (2) a glucane LCC containing ∼4% of the wood lignin; (3) a xylan-lignin-glucomannan network LCC (xylan>glucomannan) containing ∼40% of the wood lignin; and (4) a glucomannan-lignin-xylan network LCC (glucoman-nan>xylan) containing ∼48% of the wood lignin. Endoglucanase Novozyme 476, with only cellulase activity, and Ecopulp XM, with only xylanase and mannanase activities, were used as an enzymatic tool. From mildly ball-milled wood, all the lignin was isolated as LCCs. As a control, LCC was prepared from partially chlorite-delignified wood meal without ball milling, also in a mild procedure. The results were very similar to those obtained after ball milling. Thus, it can be safely concluded that the formation of new chemical linkages between lignin and carbohydrates during ball milling is improbable. Studies on isolated milled wood lignin (MWL) supported this conclusion and clearly showed that covalent linkages between lignin and carbohydrates are present. The study provide conclusive evidence of covalent linkages between lignin and carbohydrates in the native lignin in wood. It is concluded that carbohydrate-free lignin, i.e., lignin without covalent bonds to carbohydrates, probably cannot be present in spruce wood.

Holzforschung ◽  
2016 ◽  
Vol 70 (10) ◽  
pp. 911-917 ◽  
Author(s):  
Juan Tao ◽  
Takao Kishimoto ◽  
Masahiro Hamada ◽  
Noriyuki Nakajima

Abstract The potential of halogen-free and imidazolium-free phosphonium-based amino acid ionic liquids (AAILs) has been investigated as new solvents for cellulose pretreatment for the subsequent enzymatic hydrolysis of cellulose. AAILs alone did not dissolve cellulose (Avicel), even at 120°C. However, when polar solvents such as dimethylsulfoxide (DMSO) were added as cosolvents, AAILs became an acceptable solvent for cellulose at 30°C. The solubility of cellulose in tetrabutylphosphonium glycine ([TBP][Gly])/cosolvent reached 15%. The enzymatic hydrolysis of cellulose was dramatically enhanced by pretreatment with AAIL/cosolvent, and the glucose yield reached 100% when the novel AAIL tetrabutylphosphonium N,N-dimethylglycine ([TBP][DMGly]) was used in combination with DMSO as cosolvent. The enzymatic conversion of cellulose to glucose in 6% and 13% [TBP][DMGly]/DMSO buffer solutions reached 98% and 79%, respectively. The decrease in cellulase activity owing to residual [TBP][DMGly]/DMSO was not significant. Hence, it is possible to conduct the dissolution and enzymatic hydrolysis of cellulose in a one-batch process in a phosphonium-based AAIL/cosolvent system.


2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.


2013 ◽  
Vol 85 (17) ◽  
pp. 8121-8126 ◽  
Author(s):  
Britta Opitz ◽  
Andreas Prediger ◽  
Christian Lüder ◽  
Marrit Eckstein ◽  
Lutz Hilterhaus ◽  
...  

2015 ◽  
Vol 51 (52) ◽  
pp. 10502-10505 ◽  
Author(s):  
Aiping Chang ◽  
Qingshi Wu ◽  
Wenting Xu ◽  
Jianda Xie ◽  
Weitai Wu

The physical trapping of cellulose in microgels leads to a low-ordered cellulose, favoring enzymatic hydrolysis of cellulose to generate glucose.


1977 ◽  
Vol 23 (2) ◽  
pp. 139-147 ◽  
Author(s):  
D. Sternberg ◽  
P. Vuayakumar ◽  
E. T. Reese

The enzymatic conversion of cellulose is catalyzed by a multiple enzyme system. The Trichoderma enzyme system has been studied extensively and has insufficient β-glucosidase (EC 3.2.1.21) activity for the practical saccharification of cellulose. The black aspergilli (A. niger and A. phoenicis) were superior producers of β-glucosidase and a method for production of this enzyme in liquid culture is presented. When Trichoderma cellulase preparations are supplemented with β-glucosidase from Aspergillus during practical saccharifications, glucose is the predominant product and the rate of saccharification is significantly increased. The stimulatory effect of β-glucosidase appears to be due to the removal of inhibitory levels of cellobiose.


Sign in / Sign up

Export Citation Format

Share Document