Advertisement

Applied Biochemistry and Biotechnology

, Volume 188, Issue 2, pp 410–423 | Cite as

Enhanced Properties and Lactose Hydrolysis Efficiencies of Food-Grade β-Galactosidases Immobilized on Various Supports: a Comparative Approach

  • Priti Katrolia
  • Xiaolan LiuEmail author
  • Guanlong Li
  • Narasimha Kumar Kopparapu
Article
  • 67 Downloads

Abstract

In this study, a fungal and two yeast β-galactosidases were immobilized using alginate and chitosan. The biochemical parameters and lactose hydrolysis abilities of immobilized enzymes were analyzed. The pH optima of immobilized fungal β-galactosidases shifted to more acidic pH compared to free enzyme. Remarkably, the optimal temperature of chitosan-entrapped yeast enzyme, Maxilact, increased to 60 °C, which is significantly higher than that of the free Maxilact (40 °C) and other immobilized forms. Chitosan-immobilized A. oryzae β-galactosidase showed improved lactose hydrolysis (95.7%) from milk, compared to the free enzyme (82.7%) in 12 h. Chitosan-immobilized Maxilact was the most efficient in lactose removal from milk (100% lactose hydrolysis in 2 h). The immobilized lactases displayed excellent reusability, and chitosan-immobilized Maxilact hydrolyzed > 95% lactose in milk after five reuses. Compared to free enzymes, the immobilized enzymes are more suitable for cost-effective industrial production of low-lactose milk due to improved thermal activity, lactose hydrolysis efficiencies, and reusability.

Keywords

β-Galactosidase Immobilization Lactose hydrolysis Chitosan Alginate Food grade 

Notes

Funding Information

This work was supported by National Natural Science Foundation of China (Grant No. 31401628).

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflict of interest.

References

  1. 1.
    Mlichova, Z., & Rosenberg, M. (2006). Current trends of beta-galactosidase application in food technology. Journal of Food and Nutrition Research, 45(2), 47–54.Google Scholar
  2. 2.
    Bosso, A., Morioka, L. R. I., dos Santos, L. F., & Suguimoto, H. H. (2016). Lactose hydrolysis potential and thermal stability of commercial β-galactosidase in UHT and skimmed milk. Food Science and Technology (Campinas), 36(1), 159–165.  https://doi.org/10.1590/1678-457X.0085.CrossRefGoogle Scholar
  3. 3.
    Demirhan, E., Apar, D. K., & Özbek, B. (2010). A modelling study on hydrolysis of whey lactose and stability of β-galactosidase. Korean Journal of Chemical Engineering, 27(2), 536–545.  https://doi.org/10.2478/s11814-010-0062-5.CrossRefGoogle Scholar
  4. 4.
    Katrolia, P., Yan, Q., Jia, H., Li, Y., Jiang, Z., & Song, C. (2011). Molecular cloning and high-level expression of a β-galactosidase gene from Paecilomyces aerugineus in Pichia pastoris. Journal of Molecular Catalysis B: Enzymatic, 69(3–4), 112–119.  https://doi.org/10.1016/j.molcatb.2011.01.004.CrossRefGoogle Scholar
  5. 5.
    Martínez-Villaluenga, C., Cardelle-Cobas, A., Corzo, N., Olano, A., & Villamiel, M. (2008). Optimization of conditions for galactooligosaccharide synthesis during lactose hydrolysis by β-galactosidase from Kluyveromyces lactis (Lactozym 3000 L HP G). Food Chemistry, 107(1), 258–264.  https://doi.org/10.1016/j.foodchem.2007.08.011.CrossRefGoogle Scholar
  6. 6.
    Katrolia, P., Zhang, M., Yan, Q., Jiang, Z., Song, C., & Li, L. (2011). Characterisation of a thermostable family 42 β-galactosidase (BgalC) family from Thermotoga maritima showing efficient lactose hydrolysis. Food Chemistry, 125(2), 614–621.  https://doi.org/10.1016/j.foodchem.2010.08.075.CrossRefGoogle Scholar
  7. 7.
    Niu, D., Tian, X., Mchunu, N. P., Jia, C., Singh, S., Liu, X., Prior, B. A., & Lu, F. (2017). Biochemical characterization of three aspergillus Niger β-galactosidases. Electronic Journal of Biotechnology, 27, 37–43.  https://doi.org/10.1016/j.ejbt.2017.03.001.
  8. 8.
    Oliveira, C., Guimarães, P. M. R., & Domingues, L. (2011). Recombinant microbial systems for improved β-galactosidase production and biotechnological applications. Biotechnology Advances., 29(6), 600–609.  https://doi.org/10.1016/j.biotechadv.2011.03.008.CrossRefGoogle Scholar
  9. 9.
    Park, A.-R., & Oh, D.-K. (2010). Galacto-oligosaccharide production using microbial beta-galactosidase: Current state and perspectives. Applied Microbiology and Biotechnology, 85(5), 1279–1286.  https://doi.org/10.1007/s00253-009-2356-2.CrossRefGoogle Scholar
  10. 10.
    Dutra Rosolen, M., Gennari, A., Volpato, G., & Volken De Souza, C. F. (2015). Lactose hydrolysis in Milk and dairy whey using microbial β-galactosidases. Enzyme Research, 2015, 1–7.  https://doi.org/10.1155/2015/806240.CrossRefGoogle Scholar
  11. 11.
    Kumar Mukesh, D. J., Sudha, M., Devika, S., Balakumaran, M. D., Ravi Kumar, M., & Kalaichelvan, P. T. (2012). Production and optimization of β-galactosidase by Bacillus Sp. MPTK 121, isolated from dairy plant soil. Annals of. Biological Research, 3(4), 1712–1718.Google Scholar
  12. 12.
    Grosová, Z., Rosenberg, M., & Rebroš, M. (2008). Perspectives and applications of immobilised β-galactosidase in food industry - a review. Czech Journal of Food Sciences., 26(1), 1–14.CrossRefGoogle Scholar
  13. 13.
    Husain, Q. (2010). β galactosidases and their potential applications: A review. Critical Reviews in Biotechnology, 30(1), 41–62.  https://doi.org/10.3109/07388550903330497.CrossRefGoogle Scholar
  14. 14.
    Panesar, P. S., Kumari, S., & Panesar, R. (2010). Potential applications of immobilized β-galactosidase in food processing industries. Enzyme Research, 2010(16), 1–16.  https://doi.org/10.4061/2010/473137.CrossRefGoogle Scholar
  15. 15.
    DiCosimo, R., McAuliffe, J., Poulose, A. J., & Bohlmann, G. (2013). Industrial use of immobilized enzymes. Chemical Society Reviews, 42(15), 6437.  https://doi.org/10.1039/c3cs35506c.CrossRefGoogle Scholar
  16. 16.
    Mohamad, N. R., Marzuki, N. H. C., Buang, N. A., Huyop, F., & Wahab, R. A. (2015). An overview of technologies for immobilization of enzymes and surface analysis techniques for immobized enzymes. Biotechnology and Biotechnological Equipment., 29(2), 205–220.  https://doi.org/10.1080/13102818.2015.1008192.CrossRefGoogle Scholar
  17. 17.
    Zhang, D., Yuwen, L., & Peng, L. (2013). Parameters affecting the performance of immobilized enzyme. Journal of Chemistry, 2013(Article ID 946248), 7.  https://doi.org/10.1155/2013/946248.Google Scholar
  18. 18.
    Ansari, S. A., & Satar, R. (2012). Recombinant β-galactosidases - past, present and future: A mini review. Journal of Molecular Catalysis B: Enzymatic., 81, 1–6.  https://doi.org/10.1016/j.molcatb.2012.04.012.CrossRefGoogle Scholar
  19. 19.
    Datta, S., Christena, L. R., & Rajaram, Y. R. S. (2013). Enzyme immobilization: An overview on techniques and support materials. 3 Biotech, 3(1), 1–9.  https://doi.org/10.1007/s13205-012-0071-7.CrossRefGoogle Scholar
  20. 20.
    Bibi, Z., Qader, S. A. U., & Aman, A. (2015). Calcium alginate matrix increases the stability and recycling capability of immobilized endo-β-1,4-xylanase from Geobacillus stearothermophilus KIBGE-IB29. Extremophiles, 19(4), 819–827.  https://doi.org/10.1007/s00792-015-0757-y.CrossRefGoogle Scholar
  21. 21.
    Garcia-Galan, C., Berenguer-Murcia, Á., Fernandez-Lafuente, R., & Rodrigues, R. C. (2011). Potential of different enzyme immobilization strategies to improve enzyme performance. Advanced Synthesis and Catalysis., 353(16), 2885–2904.  https://doi.org/10.1002/adsc.201100534.CrossRefGoogle Scholar
  22. 22.
    Ladero, M., Santos, A., & García-Ochoa, F. (2000). Kinetic modeling of lactose hydrolysis with an immobilized β- galactosidase from Kluyveromyces fragilis. Enzyme and Microbial Technology, 27(8), 583–592.  https://doi.org/10.1016/S0141-0229(00)00244-1.CrossRefGoogle Scholar
  23. 23.
    Chen, W., Chen, H., Xia, Y., Yang, J., Zhao, J., Tian, F., Zhang, H. P., & Zhang, H. (2009). Immobilization of recombinant thermostable β-galactosidase from Bacillus stearothermophilus for lactose hydrolysis in milk. Journal of Dairy Science, 92(2), 491–498.  https://doi.org/10.3168/jds.2008-1618.CrossRefGoogle Scholar
  24. 24.
    Gürdaş, S., Güleç, H. A., & Mutlu, M. (2012). Immobilization of aspergillus oryzae β-galactosidase onto Duolite A568 resin via simple adsorption mechanism. Food and Bioprocess Technology, 5(3), 904–911.  https://doi.org/10.1007/s11947-010-0384-7.CrossRefGoogle Scholar
  25. 25.
    Roy, I., & Gupta, M. N. (2003). Lactose hydrolysis by Lactozym ™ immobilized on cellulose beads in batch and fluidized bed modes. Process Biochemistry, 39(3), 325–332.  https://doi.org/10.1016/S0032-9592(03)00086-4.CrossRefGoogle Scholar
  26. 26.
    Li, X., Zhou, Q. Z. K., & Chen, X. D. (2007). Pilot-scale lactose hydrolysis using β-galactosidase immobilized on cotton fabric. Chemical Engineering and Processing: Process Intensification, 46(5), 497–500.  https://doi.org/10.1016/j.cep.2006.02.011.CrossRefGoogle Scholar
  27. 27.
    Norouzian D.. (2003). Enzyme immobilization: The state of art in biotechnology. Iranian Journal of Biotechnology, 1(4).Google Scholar
  28. 28.
    Zhang, Z., Zhang, R., Chen, L., & McClements, D. J. (2016). Encapsulation of lactase (β-galactosidase) into k-carrageenan-based hydrogel beads: Impact of environmental conditions on enzyme activity. Food Chemistry, 200(June), 69–75.  https://doi.org/10.1016/j.foodchem.2016.01.014.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.College of Food and Biological EngineeringQiqihar UniversityQiqiharPeople’s Republic of China

Personalised recommendations