Impact of the Supramolecular Structure of Cellulose on the Efficiency of Enzymatic Hydrolysis

Overview

Journal Biotechnol Biofuels

Publisher Biomed Central

Specialty Biotechnology

Date 2015 Apr 15

PMID 25870653

Citations 20

Authors

Ausra Peciulyte

Katarina Karlstrom

Per Tomas Larsson

Lisbeth Olsson

Affiliations

Soon will be listed here.

Abstract

Background: The efficiency of enzymatic hydrolysis is reduced by the structural properties of cellulose. Although efforts have been made to explain the mechanism of enzymatic hydrolysis of cellulose by considering the interaction of cellulolytic enzymes with cellulose or the changes in the structure of cellulose during enzymatic hydrolysis, the process of cellulose hydrolysis is not yet fully understood. We have analysed the characteristics of the complex supramolecular structure of cellulose on the nanometre scale in terms of the spatial distribution of fibrils and fibril aggregates, the accessible surface area and the crystallinity during enzymatic hydrolysis. Influence of the porosity of the substrates and the hydrolysability was also investigated. All cellulosic substrates used in this study contained more than 96% cellulose.

Results: Conversion yields of six cellulosic substrates were as follows, in descending order: nano-crystalline cellulose produced from never-dried soda pulp (NCC-OPHS-ND) > never-dried soda pulp (OPHS-ND) > dried soda pulp (OPHS-D) > Avicel > cotton treated with sodium hydroxide (cotton + NaOH) > cotton.

Conclusions: No significant correlations were observed between the yield of conversion and supramolecular characteristics, such as specific surface area (SSA) and lateral fibril dimensions (LFD). A strong correlation was found between the average pore size of the starting material and the enzymatic conversion yield. The degree of crystallinity was maintained during enzymatic hydrolysis of the cellulosic substrates, contradicting previous explanations of the increasing crystallinity of cellulose during enzymatic hydrolysis. Both acid and enzymatic hydrolysis can increase the LFD, but no plausible mechanisms could be identified. The sample with the highest initial degree of crystallinity, NCC-OPHS-ND, exhibited the highest conversion yield, but this was not accompanied by any change in LFD, indicating that the hydrolysis mechanism is not based on lateral erosion.

Citing Articles

Structural changes and cellulose ultrastructure mapped with electron microscopy and SAXS after enzymatic hydrolysis of mildly steam pretreated Norway spruce.

Brollo M, Caputo F, Naidjonoka P, Olsson L, Olsson E Biotechnol Biofuels Bioprod. 2025; 18(1):19.

PMID: 39984976 PMC: 11846163. DOI: 10.1186/s13068-025-02616-7.

Enzymatic functionalization of bacterial nanocellulose: current approaches and future prospects.

Kaczmarek M, Bialkowska A J Nanobiotechnology. 2025; 23(1):82.

PMID: 39905460 PMC: 11796255. DOI: 10.1186/s12951-025-03163-x.

The Effect of Accessibility of Insoluble Substrate on the Overall Kinetics of Enzymatic Degradation.

Petrasek Z, Nidetzky B Biotechnol Bioeng. 2025; 122(4):895-907.

PMID: 39763056 PMC: 11895425. DOI: 10.1002/bit.28921.

Investigating the role of AA9 LPMOs in enzymatic hydrolysis of differentially steam-pretreated spruce.

Caputo F, Tolgo M, Naidjonoka P, M Krogh K, Novy V, Olsson L Biotechnol Biofuels Bioprod. 2023; 16(1):68.

PMID: 37076886 PMC: 10114483. DOI: 10.1186/s13068-023-02316-0.

Different particle size study of castor deoiled cake for biofuel production with an environmental sustainability perspective.

Deshmukh M, Pande A, Marathe A Heliyon. 2022; 8(6):e09710.

PMID: 35756129 PMC: 9213708. DOI: 10.1016/j.heliyon.2022.e09710.

References

Fitzpatrick M, Champagne P, Cunningham M, Whitney R . A biorefinery processing perspective: treatment of lignocellulosic materials for the production of value-added products. Bioresour Technol. 2010; 101(23):8915-22. DOI: 10.1016/j.biortech.2010.06.125. View

Liu Y, Baker J, Zeng Y, Himmel M, Haas T, Ding S . Cellobiohydrolase hydrolyzes crystalline cellulose on hydrophobic faces. J Biol Chem. 2011; 286(13):11195-201. PMC: 3064174. DOI: 10.1074/jbc.M110.216556. View

Bergenstrahle M, Wohlert J, Larsson P, Mazeau K, Berglund L . Dynamics of cellulose-water interfaces: NMR spin-lattice relaxation times calculated from atomistic computer simulations. J Phys Chem B. 2008; 112(9):2590-5. DOI: 10.1021/jp074641t. View

Igarashi K, Uchihashi T, Koivula A, Wada M, Kimura S, Okamoto T . Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface. Science. 2011; 333(6047):1279-82. DOI: 10.1126/science.1208386. View

Zeng Y, Zhao S, Yang S, Ding S . Lignin plays a negative role in the biochemical process for producing lignocellulosic biofuels. Curr Opin Biotechnol. 2014; 27:38-45. DOI: 10.1016/j.copbio.2013.09.008. View

Ding S, Xu Q, Ali M, Baker J, Bayer E, Barak Y . Versatile derivatives of carbohydrate-binding modules for imaging of complex carbohydrates approaching the molecular level of resolution. Biotechniques. 2006; 41(4):435-6, 438, 440 passim. DOI: 10.2144/000112244. View

Otero J, Panagiotou G, Olsson L . Fueling industrial biotechnology growth with bioethanol. Adv Biochem Eng Biotechnol. 2007; 108:1-40. DOI: 10.1007/10_2007_071. View

Yu Z, Jameel H, Chang H, Philips R, Park S . Evaluation of the factors affecting avicel reactivity using multi-stage enzymatic hydrolysis. Biotechnol Bioeng. 2011; 109(5):1131-9. DOI: 10.1002/bit.24386. View

Tormo J, Lamed R, Chirino A, Morag E, Bayer E, Shoham Y . Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 1996; 15(21):5739-51. PMC: 452321. View

10.

Hemsworth G, Henrissat B, Davies G, Walton P . Discovery and characterization of a new family of lytic polysaccharide monooxygenases. Nat Chem Biol. 2013; 10(2):122-6. PMC: 4274766. DOI: 10.1038/nchembio.1417. View

11.

Peciulyte A, Anasontzis G, Karlstrom K, Larsson P, Olsson L . Morphology and enzyme production of Trichoderma reesei Rut C-30 are affected by the physical and structural characteristics of cellulosic substrates. Fungal Genet Biol. 2014; 72:64-72. DOI: 10.1016/j.fgb.2014.07.011. View

12.

Chandra R, Bura R, Mabee W, Berlin A, Pan X, Saddler J . Substrate pretreatment: the key to effective enzymatic hydrolysis of lignocellulosics?. Adv Biochem Eng Biotechnol. 2007; 108:67-93. DOI: 10.1007/10_2007_064. View

13.

Ooshima H, Kurakake M, Kato J, Harano Y . Enzymatic activity of cellulase adsorbed on cellulose and its change during hydrolysis. Appl Biochem Biotechnol. 1991; 31(3):253-66. DOI: 10.1007/BF02921752. View

14.

Hall M, Bansal P, Lee J, Realff M, Bommarius A . Cellulose crystallinity--a key predictor of the enzymatic hydrolysis rate. FEBS J. 2010; 277(6):1571-82. DOI: 10.1111/j.1742-4658.2010.07585.x. View

15.

Ohad I, DANON I, HESTRIN S . Synthesis of cellulose by Acetobacter xylinum. V. Ultrastructure of polymer. J Cell Biol. 1962; 12:31-46. PMC: 2106003. DOI: 10.1083/jcb.12.1.31. View

16.

Gilkes N, Kilburn D, Miller Jr R, Warren R, Sugiyama J, Chanzy H . Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose. Int J Biol Macromol. 1993; 15(6):347-51. DOI: 10.1016/0141-8130(93)90052-n. View

17.

Pauly M, Keegstra K . Cell-wall carbohydrates and their modification as a resource for biofuels. Plant J. 2008; 54(4):559-68. DOI: 10.1111/j.1365-313X.2008.03463.x. View

18.

Kohnke T, Ostlund A, Brelid H . Adsorption of arabinoxylan on cellulosic surfaces: influence of degree of substitution and substitution pattern on adsorption characteristics. Biomacromolecules. 2011; 12(7):2633-41. DOI: 10.1021/bm200437m. View

19.

Park S, Baker J, Himmel M, Parilla P, Johnson D . Cellulose crystallinity index: measurement techniques and their impact on interpreting cellulase performance. Biotechnol Biofuels. 2010; 3:10. PMC: 2890632. DOI: 10.1186/1754-6834-3-10. View

20.

Ding S, Himmel M . The maize primary cell wall microfibril: a new model derived from direct visualization. J Agric Food Chem. 2006; 54(3):597-606. DOI: 10.1021/jf051851z. View