Alcalase immobilization onto chitosan/glutaraldehyde/tripolyphosphate beads obtained by inverse emulsion technique

Original scientific paper

Authors

  • Milena Žuža Praštalo Department of Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, 11000 Belgrade, Serbia
  • Nikola Milašinović Department of Forensic Sciences, Faculty of Forensic Sciences and Engineering, University of Criminal Investigation and Police Studies, Cara Dušana 196, 11080 Belgrade, Serbia
  • Marko Jonović Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Njegoševa 12, 11000 Belgrade, Serbia
  • Melina Kalagasidis-Krušić Department of Organic Chemical Technology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, 11000 Belgrade, Serbia
  • Zorica Knežević-Jugović Department of Biochemical Engineering and Biotechnology, Faculty of Technology and Metallurgy, University of Belgrade, Karnegijeva 4, 11000 Belgrade, Serbia

DOI:

https://doi.org/10.2298/CICEQ240401037Z

Keywords:

Alcalase® 2.4L, covalent immobilization, inverse emulsion technique, chitosan beads, tripolyphosphate

Abstract

Enzymes immobilization can efficiently solve limitations of their large-scale application, such as stability and reusability. In this study, Alcalase® 2.4L (protease from Bacillus licheniformis) was covalently immobilized onto chitosan beads obtained by inverse emulsion technique using 1.5% (m/v) of chitosan and 0.67 % (v/v) or 1.0 % (v/v) of glutaraldehyde (CTPP (1.5/0.67) and CTPP (1.5/1.0)). Afterwards, the beads were additionally crosslinked by immersion into 10 % (m/v) tripolyphosphate solution. Parameters studied were enzyme loading, enzyme coupling yield, beads diameter, SEM, biocatalyst activity and FTIR. The beads had adequate enzyme loading and enzyme coupling yield (Pgmax was 117.1 mg/g dry CTPP 1.5/0.67 and 90.1 mg/g dry CTPP 1.5/1.0; and hmax was 96.7 % for both carriers). CTPP (1.5/1.00) beads were smaller (diameter 635.2 ±25.2 mm wet/ 230.4±12.5 mm dry beads) and showed higher specific activity of 20.1 ± 0.23 IU/mgprotein. The immobilized Alcalase® 2.4L was tested for hydrolysing egg white and soy proteins. Alcalase® 2.4L, covalently attached to CTTP (1.5/1.0) chitosan beads, is a promising choice for industrial processes involving egg white protein hydrolysis, as the enzyme achieved a notable hydrolysis rate of 26.34 ± 0.879 % after 195 minutes. Additionally, it remained effective through five successive applications under practical conditions (50 °C, pH 8).

References

[1] C. Liu, M. Bhattarai, K. S. Mikkonen, M. Heinonen, J. Agric. Food Chem. 67 (2019) 6625–6632. https://doi.org/10.1021/acs.jafc.9b00914.

[2] A. Eberhardt, E. C. López, R. J. Ceruti, F. Marino, E. J. Mammarella, R. M. Manzo, G. A. Sihufe, Int. J. Dairy Technol. 72 (2019) 573–584. https://doi.org/10.1111/1471-0307.12606.

[3] F. Hussain, S. Arana-Peña, R. Morellon-Sterling, O. Barbosa, S. A. Braham, S. Kamal, R. Fernandez-Lafuente, Molecules. 23 (2018) 3188. https://doi.org/10.3390/molecules23123188.

[4] A. S. S. Ibrahim, A. A. Al-Salamah, A. M. El-Toni, K. S. Almaary, M. A. El-Tayeb, Y. B. Elbadawi, G. Antranikian, Int. J. Mol. Sci. 17 (2016) 184. https://doi.org/10.3390/ijms17020184.

[5] M. G. Žuža, N. Z. Milašinović, M. M. Jonović, J. R. Jovanović, M. T. Kalagasidis Krušić, B. M. Bugarski, Z. D. Knežević-Jugović, Bioprocess Biosyst. Eng. 40 (2017) 1713–1723. https://doi.org/10.1007/s00449-017-1826-7.

[6] Y. Aslan, A. Y. Taher, I. Cavidoğlu, J. Anim. Plant Sci. 28 (2018) 1648–1655. https://www.siirt.edu.tr/dosya/personel/alan-taher-yaseen-ile-makale-siirt-2019226111612272.pdf

[7] P. J. Allertz, S. Berger, G. Sellenk, C. Dittmer, M. Dietze, K. P. Stahmann, K. Salchert, Catalysts. 7 (2017) 1–21. https://doi.org/10.3390/catal7120359.

[8] R. Plagemann, J. von Langermann, U. Kragl, Eng. Life Sci. 14 (2014) 493–499. https://doi.org/10.1002/elsc.201300115.

[9] M. Planchestainer, D. R. Padrosa, M. L. Contente, F. Paradisi, Catalysts. 8 (2018) 40. https://doi.org/10.3390/catal8010040.

[10] P. Zucca, E. Sanjust, Molecules. 19 (2014) 14139–14194. https://doi.org/10.3390/molecules190914139.

[11] M. G. Žuža, S. Šiler-Marinković, Z. D. Knežević-Jugović, Chem. Ind. Chem. Eng. Q. 13 (2007) 205-210. https://doi.org/10.2298/CICEQ0704205Z.

[12] S. Ait Braham, F. Hussain, R. Morellon-Sterling, S. Kamal, J. F. Kornecki, O. Barbosa, D. E. Kati, R. Fernandez-Lafuente, Biotechnol. Prog. 35 (2019) 1–4. https://doi.org/10.1002/btpr.2768.

[13] L. Molawa, J. Jordaan, J. Limson, D. Brady, Biocatal. Biotransform. 31 (2013) 71–78. https://doi.org/10.3109/10242422.2013.767335.

[14] C. Fenoglio, N. Vierling, R. Manzo, R. Ceruti, G. Sihufe, E. Mammarella, Am. J. Food Technol. 11 (2016) 152–158. https://doi.org/10.3923/ajft.2016.152.158.

[15] T. B. Pessato, N. C. de Carvalho, O. L. Tavano, L. G. R. Fernandes, R. de L. Zollner, F. M. Netto, Food Res. Int. 83 (2016) 112–120. https://doi.org/10.1016/j.foodres.2016.02.015.

[16] Y. Liu, D. Dave, Aquaculture. 548 (2022) 737546. https://doi.org/10.1016/j.aquaculture.2021.737546.

[17] T. A. Siswoyo, N. F. Matra, A. A. Safiera, A. Supriyadi, IJASEIT. 7 (2017) 1315–1321. https://doi.org/10.18517/ijaseit.7.4.936.

[18] S. nan Wang, C. ran Zhang, B. kun Qi, X. nan Sui, L. zhou Jiang, Y. Li, Z. jiang Wang, H. xia Feng, R. Wang, Q. zhi Zhang, Eur. Food Res. Technol. 239 (2014) 1051–1059. https://doi.org/10.1007/s00217-014-2301-1.

[19] H. Zhu, Y. Zhang, T. Yang, D. Zheng, X. Liu, J. Zhang, LWT. 162 (2022) 113505. https://doi.org/10.1016/j.lwt.2022.113505.

[20] P. dos S. Kimberle, M. S. Carolina, I. S. B. Ana, R. B. G. Luciana, Process Biochem. 97 (2020) 27–36. https://doi.org/10.1016/j.procbio.2020.06.019.

[21] M. Jonović, M. Žuža, V. Ðorđević, N. Šekuljica, M. Milivojević, B. Jugović, B. Bugarski, Z. Knežević-Jugović, Catalysts. 11 (2021) 1–17. https://doi.org/10.3390/catal11030305.

[22] Q. Zeng, Q. Li, D. Sun, M. Zheng, Front. bioeng. biotechnol. 8 (2020) 1–11. https://doi.org/10.3389/fbioe.2020.00565.

[23] Y. Qin, P. Li, Int. J. Mol. Sci. 21 (2020) 499. https://doi.org/10.3390/ijms21020499.

[24] M. Gierszewska-Drużyńska, J. Ostrowska-Czubenko, Prog. Chem. Appl. Chitin Its Deriv. 20 (2015) 43–53. https://doi.org/10.15259/PCACD.20.04.

[25] D. Svirskis, A. Seyfoddin, S. Chalabi, J. H. I. Kim, C. Langford, S. Painter, R. Al-Kassas, Pharm. Dev. Technol. 19 (2014) 571–576. https://doi.org/10.3109/10837450.2013.813539.

[26] M. I. Wahba, Biotechnol. Prog. 34 (2018) 347–361. https://doi.org/10.1002/btpr.2587.

[27] S. K. Yong, M. Shrivastava, P. Srivastava, A. Kunhikrishnan, N. Bolan, Rev Environ Contam Toxicol. 233 (2015) 1-43. doi: 10.1007/978-3-319-10479-9_1

[28] W. Zeng, H. Hui, Z. Liu, Z. Chang, M. Wang, B. He, D. Hao, Carbohydr Polym. 258 (2021) 117684. DOI: 10.1016/j.carbpol.2021.117684

[29] C. Pan, J. Qian, C. Zhao, H. Yang, X. Zhao, H. Guo, Carbohydr Polym. 241 (2020) 116349. https://doi.org/10.1016/j.carbpol.2020.116349

[30] S. Durkut, Y. M. Elcin, A. E. Elcin, Artif Cells Blood Substit Immobil Biotechnol. 34 (2) (2006) 263–276.

[31] M. G. Žuža, B. M. Obradović, Z. D. Knežević-Jugović, Chem. Eng. Technol. 34 (2011) 1706–1714. https://doi.org/10.1002/ceat.201100297.

[32] M. M. Bradford, Anal. Biochem. 72 (1976) 248–254. https://doi: 10.1016/0003-2697(76)90527-3.

[33] G. Sarath, R. de la Motie, F. Wagner, in Proteolytic Enzymes: A Practical Approach, R. Beynon, J. Bond Editors, IRL Press, Oxford (1989), 25-56. ISBN 0-19-963058-5/963059-3.

[34] J. Adler-Nissen, Enzymatic hydrolysis of food proteins, Elsevier Applied Science Publishers, London and New York (1989), p 427.

[35] N. S. Rios, S. Arana-Peña, C. Mendez-Sanchez, Y. Lokha, V. Cortes-Corberan, L. R. B. Gonçalves, R. Fernandez-Lafuente, Catalysts. 9 (2019) 576. https://doi.org/10.3390/catal9070576.

[36] R. Austin, Enzyme Immobilization, ED-TECH PRESS, United Kingdom (2018), p. 181.

[37] L. N. Corîci, A. E. Frissen, D. J. Van Zoelen, I. F. Eggen, F. Peter, C. M. Davidescu, C. G. Boeriu, J. Mol. Catal. B: Enzym. 73 (2011) 90–97. https://doi.org/10.1016/j.molcatb.2011.08.004.

[38] L. Ferreira, M. A. Ramos, J. S. Dordick, M. H. Gil, J. Mol. Catal. B: Enzym. 21 (2003) 189–199. https://doi.org/10.1016/S1381-1177(02)00223-0.

[39] P. W. Tardioli, J. Pedroche, R. L. C. Giordano, R. Fernández-Lafuente, J. M. Guisán, Biotechnol. Prog. 19 (2003) 352–360. https://doi.org/10.1021/bp025588n.

[40] U. M. F. de Oliveira, L. J. B. Lima de Matos, M. C. M. de Souza, B. B. Pinheiro, J. C. S. dos Santos, L. R. B. Gonçalves, Appl. Biochem. Biotechnol. 184 (2018) 1263–1285. https://doi.org/10.1007/s12010-017-2622-1.

[41] S. D. Gür, N. İdil, N. Aksöz, Appl. Biochem. Biotechnol. 184 (2018) 538–552. https://doi.org/10.1007/s12010-017-2566-5.

[42] A. K. Sharma, B. A. Kikani, S. P. Singh, Int. J. Biol. Macromol. 153 (2020) 680–696. https://doi.org/10.1016/j.ijbiomac.2020.03.006.

[43] S. Ranjbari, A. Ayati, B. Tanhaei, A. Al-Othman, F. Karimi, Environ. Res. 204 (2022) 111961. https://doi.org/10.1016/j.envres.2021.111961.

[44] B. E. Abdelmalek, A. Sila, A. Haddar, A. Bougatef, M. A. Ayadi, Int. J. Biol. Macromol., 104 (2017) 953–962. https://doi.org/10.1016/j.ijbiomac.2017.06.107.

[45] S. Najavand, M. Habibnejad, A. R. Amani-Ghadim, P. Rahimizadeh, M. Pazhang, Biotechnol. Prog. 36 (2020) 2960. https://doi.org/10.1002/btpr.2960.

[46] M. A. A. Abdella, G. M. El-Sherbiny, A. R. El-Shamy, S. M. M. Atalla, S. A. Ahmed, Bull. Natl. Res. Cent. 44 (2020) 40. https://doi.org/10.1186/s42269-020-00301-3.

Cover

Downloads

Published

10.12.2024

Issue

Articles in Press

Section

Articles

License

Copyright (c) 2023 Milena Žuža Praštalo , Nikola Milašinović, Marko Jonović, Melina Kalagasidis-Krušić , Zorica Knežević-Jugović

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Authors who publish with this journal agree to the following terms:

Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.

Authors grant to the Publisher the following rights to the manuscript, including any supplemental material, and any parts, extracts or elements thereof:

  • the right to reproduce and distribute the Manuscript in printed form, including print-on-demand;
  • the right to produce prepublications, reprints, and special editions of the Manuscript;
  • the right to translate the Manuscript into other languages;
  • the right to reproduce the Manuscript using photomechanical or similar means including, but not limited to photocopy, and the right to distribute these reproductions;
  • the right to reproduce and distribute the Manuscript electronically or optically on any and all data carriers or storage media – especially in machine readable/digitalized form on data carriers such as hard drive, CD-Rom, DVD, Blu-ray Disc (BD), Mini-Disk, data tape – and the right to reproduce and distribute the Article via these data carriers; 
  • the right to store the Manuscript in databases, including online databases, and the right of transmission of the Manuscript in all technical systems and modes;
  • the right to make the Manuscript available to the public or to closed user groups on individual demand, for use on monitors or other readers (including e-books), and in printable form for the user, either via the internet, other online services, or via internal or external networks.

How to Cite

Alcalase immobilization onto chitosan/glutaraldehyde/tripolyphosphate beads obtained by inverse emulsion technique: Original scientific paper. (2024). Chemical Industry & Chemical Engineering Quarterly. https://doi.org/10.2298/CICEQ240401037Z

Similar Articles

61-70 of 123

You may also start an advanced similarity search for this article.