Methods for pre-processing cane to obtain enzymative hydrolysates with high sugar content

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription Access

Abstract

Methods of cane pretreatment (grinding, hydrothermal treatment, treatment with acid or alkali solutions, organosolv, deep eutectic solvents) and their effect on its subsequent enzymatic hydrolysis by cellulases and hemicellulases complexes have been studied. Substrates with the highest reactivity were obtained by exposing the cane to a weakly alkaline deep eutectic solvent (DES) and an alkali solution. The depth of enzymatic hydrolysis of these pretreated substrates was 63 and 59%, and the degree of conversion of polysaccharides (cellulose and hemicellulose) into monosaccharides taking into account the yield of the substrate at the pre-processing stage was 60 and 34%, respectively. After pre-treatment of the cane with acid DES, water steam, water or water/organic solution of sulfuric acid the depth of enzymatic hydrolysis was 45, 25, 20 and 11%, and the degree of polysaccharide conversion was 26, 18, 13 and 10%, respectively. The industrial enzyme preparation Agrocell Plus with a predominant content of cellobiohydrolases and endoglucanases was most effective in hydrolyzing the dust fraction of cane, as well as cane pretreated with a solution of sulfuric acid or DES (acidic or alkaline). The industrial enzyme preparation Agroxil Plus, containing endoxylanase and cellobiohydrolases, was more effective in hydrolyzing cane after hydrothermal pretreatment or alkali solution. The results of the hydrolysis of cane pretreated with acidic or weakly alkaline DES under the action of individual (homogeneous) cellulases indicate that in both cases the key enzyme was cellobiohydrolase 1.

Full Text

Restricted Access

About the authors

M. V. Semenova

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

A. M. Rozhkova

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Author for correspondence.
Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

D. O. Osipov

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

V. D. Telitsin

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

E. A. Rubtsova

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

E. G. Kondrat’eva

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

I. S. Vasil’eva

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

O. V. Morozova

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

A. I. Yaropolov

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

A. P. Sinitsyn

Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences

Email: amrojkova@yahoo.com
Russian Federation, Moscow, 119071

References

  1. Гусаков А.В., Синицын А.П. // Химия биомассы: биотоплива и биопластики. М.: Научный мир, 2017. 789 с. ISBN 978-5-91522-451-2
  2. Количественный химический анализ растительного сырья. / Ред. В.И. Шарков, И.И. Куйбина, Ю.П. Соловьева, Т.А. Павлова. М.: Лесная промышленность, 1976. С. 63–64.
  3. Dibyajyoti H., Kumar P. // Process Biochem. 2020. V. 89. P. 110–133. https://doi.org/10.1016/j.procbio.2019.10.001
  4. Gusakov A.V. // Biofuels. 2013. V. 4. № 6. P. 567–569. https://doi.org/10.4155/bfs.13.55
  5. Teter S.A., Brandon S.K., Emme B. Enzymatic Processes and Enzyme Development in Diorefining // Advances in Biorefineries. 2014. P. 199–233. https://doi.org/10.1533/9780857097385.1.199
  6. Sun Q., Foston M., Meng X., Sawada D., Pingali S.V., O’Neill H. M.,et al. // Biotechnol. Biofuels. 2014. V. 7. № 150. P. 1–14. https://doi.org/10.1186/s13068- 014-0150-6
  7. Yang B., Dai Z., Ding S.-Y., Wyman C.E. // Biofuels. 2011. V. 2. № 4. P. 421–449. https://doi.org/10.4155/bfs.11.116
  8. Kumar P., Barrett D.M., Delwiche M.J., Stroeve P. // Ind. Eng. Chem. Res. 2009. V. 48. P. 3713–3729. https://doi.org/10.1021/ie801542g
  9. Karimi K., Taherzadeh M.J. // Bioresour. Technol. 2016. V. 200. P. 1008–1018. https://doi.org/10.1016/j.biortech.2015.11.022
  10. Liguori R., Ventorino V., Pepe O., Faraco V. // Appl. Microbiol. Biotechnol. 2016. V. 100. № 2. P. 597–611. https://doi.org/10.1007/s00253-015-7125-9
  11. He Y.-C., Ma C.-L., Yang B. // Fungal Cellulolytic Enzymes. Microbial production and application. / Ed. Xu Fang, Yinbo Qu. Springer. 2018. P. 1–25. https://doi.org/10.1007/978-981-13-0749-2_1
  12. Alvira P., Tomáspejó E., Ballesteros M., Negro M.J. // Bioresour. Technol. 2010. V. 101. № 13. P. 4851–4861. https://doi.org/10.1016/j.biortech.2009.11.093
  13. Paudel S.R., Banjara S.P., Choi O.K., Park K.Y., Kim Y.M., Lee J.W. // Bioresour. Technol. 2017. V. 245. P. 1194–1205. https://doi.org/10.1016/j.biortech.2017.08.182
  14. Hideno A., Inoue H., Tsukahara K., Fujimoto S., Minowa T. Inoue S., Endo T., Sawayama S. // Bioresour. Technol. 2009. V. 100. P. 2706–2711. https://doi.org/10.1016/j.biortech.2008.12.057
  15. Ghizzi G., Silva D., Couturier M., Berrin J.-G., Buléon A., Rouau, X. // Bioresour. Technol. 2012. V. 103. P. 192–210. https://doi.org/10.1016/j.biortech.2011.09.073
  16. Bobleter O., Concin R. // Cellulose Chemistry and Technol. 1979. V. 13. P. 583–593.
  17. Павлов И.Н. // Ползуновский вестник. 2018. № 1. С. 148–152. https://doi.org/10.25712/ASTU.2072-8921.2018.01.028
  18. Bali G., Meng X., Deneff J.I., Sun Q., Ragauskas A.J. // ChemSusChem. 2015. V. 8. P. 275–279. https://doi.org/10.1002/cssc.201402752
  19. Prajapati B.P., Jana U.K., Suryawanshi R.K., Kango N. // Renewable Energy. 2020. V. 152. P. 653–663. https://doi.org/10.1016/j.renene.2020.01.063
  20. Liu I., Li Z. // RSC Advances. 2017. V. 7. P. 47456–47463. https://doi.org/10.1039/C7RA08101D
  21. Qing Q., Zhou L.L., Guo Q., Huang M.Z., He Y.C., Wang L.Q., Zhang Y. // Bioresour. Technol. 2016. V. 218. P. 209–216. https://doi.org/10.1016/j.biortech.2016.06.063
  22. Rabemanolontsoa H., Saka S. // Bioresour. Technol. 2016. V. 199. P. 83–91. https://doi.org/10.1016/j.biortech.2015.08.029
  23. Mishra A., Ghosh S. // Fuel. 2019. V. 236. P. 544–553. https://doi.org/10.1016/j.fuel.2018.09.024
  24. Woiciechowski A. L., Dalmas Neto C.J., Vandenberghe L.P.S., Carvalho Neto D.P., Sydney A.C.N., Letti L.A.J. et al. // Bioresour. Technol. 2020. V. 304. 122848. https://doi.org/10.1016/j.biortech.2020.122848
  25. Yu Z., Du Y., Shang X., Zheng Y., Zhou J. // Industrial Crops and Products. 2018. V. 124. P. 555–562. https://doi.org/10.1016/j.indcrop.2018.08.029
  26. Nitsos C., Matsakas L., Triantafyllidis K., Rova U., Christakopoulos P. // Biofuels. 2018. V. 9. P. 545–558. https://doi.org/10.1080/17597269.2017.1378988
  27. Liu Q., Li W., Ma Q., An S., Li M., Jameel H., Chang H.M. // Bioresour. Technol. 2016. V. 211. P. 435–442. https://doi.org/10.1016/j.biortech.2016.03.131
  28. Ostovareh S., Karimi K., Zamani A. // Industrial Crops and Products. 2015. V. 66. P. 170–177. https://doi.org/10.1016/j.indcrop.2014.12.023
  29. He Y.C., Liu F., Di J.H., Ding Y., Tao Z.C., Zhu Z.Z. et al.. // Industrial Crops and Products. 2016. V. 81. P. 129–138. https://doi.org/10.1016/j.indcrop.2015.11.079
  30. Arato C., Kendall P., Gjennstad G. // Appl. Biochem. and Biotechnol. 2005. V. 123. P. 871–882. https://doi.org/10.1007/978-1-59259-991-2_74
  31. Satlewal A., Agrawal R., Bhagia S., Sangoro J., Ragauskas A.J. // Biotechnol. Adv. 2018. V. 3. P. 2032–2050. https://doi.org/10.1016/j.biotechadv.2018.08.009
  32. Zhao H., Baker G.A. // J. Chemical Technol. and Biotechnol. 2012. V. 88. P. 3–12. https://doi.org/10.1002/jctb.3935
  33. New E.K., Wu T.Y., Lee C.B., Poon Z.Y., Loow Y.-L., Foo L.Y.W. et al. // Process Safety and Environmental Protection. 2019. V. 123. P. 190–198. https://doi.org/10.1016/j.psep.2018.11.015
  34. Chen Z., Jacoby W.A., Wan C. // Bioresour. Technol. 2019. V. 279. P. 281–286. https://doi.org/10.1016/j.biortech.2019.01.126
  35. Chong G., Di J., Ma C., Wang D., Wang C., Wang L., Zhang P., Zhu J., He Y. // Bioresour. Technol. 2018. V. 261. P. 196–205. https://doi.org/10.1016/j.biortech.2018.04.015
  36. Синицын А.П., Синицына О.А. // Успехи биологической химии. 2021. Т. 61. С. 347–414.
  37. Morozova V.V., Gusakov A.V., Andrianov R.M., Pravilnikov A.G., Osipov D.O., Sinitsyn A.P. // Biotechnol. J. 2010. V. 5. № 8. P. 871–880. https://doi.org/10.1002/biot.201000050
  38. Dotsenko G.S., Gusakov A.V., Rozhkova A.M., Korotkova O.G., Sinitsyn A.P. // Process Biochem. 2015. V. 50. P. 1258–1263. https://doi.org/10.1016/j.procbio.2015.05.008
  39. Синицын А.П., Черноглазов В.М., Гусаков А.В. Итоги науки и техники. М.: ВИНИТИ, Биотехнология. 1990. № 25. С. 148.
  40. Korotkova O.G., Semenova M.V., Morozova V.V., Zorov I.N., Sokolova L.M., Bubnova T.M. et al. // Biochemistry (Moscow). 2009. V. 74. № 5. P. 569–577. https://doi.org/10.1134/S0006297909050137
  41. Синицына О.А., Бухтояров Ф.Е., Гусаков А.В., Окунев О.Н., Беккаревич А.О. и др. // Биохимия. 2003. Т. 68. № 11. С. 1494–1505.
  42. Осипов Д.О., Булахов А.Г., Короткова О.Г., Рожкова А.М., Дуплякин Е.О. и др. // Катализ в промышленности. 2016. Т. 16. С. 75–82. https://doi.org/10.18412/1816-0387-2016-5-75-82
  43. Procentese A., Johnson E., Orr V., Garruto Campanile A., Wood J.A., Marzocchella A. et al. // Biores. Technol. 2015. V. 192. P. 31–36. https://doi.org/10.1016/j.biortech.2015.05.053
  44. Zhang C.-W., Xia S.-Q., Ma P.-S. // Biores. Technol. 2016. V. 219. P. 1–5. https://doi.org/10.1016/j.biortech.2016.07.026
  45. Wahlstrom R., Hiltunen J., Pitaluga De Souza Nascente Sirkka M., Vuoti S., Kruus K. // RSC Adv. 2016. V. 6. № 72. P. 68100–68110. https://doi.org/10.1039/C6RA11719H
  46. Семенова М.В., Васильева И.С., Ярополов А.И., Синицын А.П. // Прикл. биохимия микробиология. 2023. Т. 59. №3. С. 253–259. https://doi.org/10.31857/S0555109923030169
  47. Синицын А.П., Осипов Д.О., Цурикова Н.В., Великорецкая И.А., Шашков И.А., Зверев С.В. // Биотехнология. 2016. Т. 1. С. 27–36. https://doi.org/10.21519/0234-2758-2016-1-27-36
  48. Доценко Г.С., Осипов Д.О., Зоров И.Н., Синицын А.П. // Катализ в промышленности. 2015. Т. 15. С. 67–73. https://doi.org/10.18412/1816-0387-2015-5-67-73

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2. Fig. 1. Reed with different degrees of grinding in a knife mill: 1 – dust fraction, 2 – coarse fraction, 3 – original reed.

Download (285KB)
Indexing metadata
3. Fig. 2. Depth of hydrolysis of coarse (1) and dust fractions (2) of crushed reed after 48 hours of treatment with FP Agrocell Plus (10 mg protein/g substrate) and F10 (1 mg protein/g substrate) at 50°C, pH 5.0. The abscissa shows the substrate concentration.

Download (55KB)
Indexing metadata
4. Fig. 3. Concentration of BC after 48 h of hydrolysis of reed (40 g/l), pretreated with GER HCHL with MK (1) or MEA (2), under the action of purified enzymes (10 mg protein/g substrate) with the addition of β-glucosidase (1 mg protein/g substrate) at 50°C, pH 5.0: CBH – cellobiohydrolase, EG – endoglucanase, EC – endoxylanase.

Download (51KB)
Indexing metadata
5. Fig. 4. Concentration of BC after 48 h of hydrolysis of cane (40 g/l) pretreated with GER XXl with MK (1, 2) or MEA (3, 4), under the action of mixtures of purified enzymes (4.5 mg total protein/g substrate) with the addition of β-glucosidase (0.45 mg protein/g substrate) at 50°C, pH 5.0: 1 and 3 – mixtures of CBG with EG; 1, 2 and 4 – with EC. The abscissa axis shows the percentage content of cellobiohydrolases in the mixtures relative to the total enzyme content.

Download (84KB)
Indexing metadata

Copyright (c) 2024 Russian Academy of Sciences