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

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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.

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References

  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.

    CAS  Google Scholar 

  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.

    Article  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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. 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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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. 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.

    Article  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  PubMed  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  PubMed  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  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.

    Article  CAS  Google Scholar 

  27. Norouzian D.. (2003). Enzyme immobilization: The state of art in biotechnology. Iranian Journal of Biotechnology, 1(4).

  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.

    Article  CAS  PubMed  Google Scholar 

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Funding

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

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Authors and Affiliations

  1. College of Food and Biological Engineering, Qiqihar University, Qiqihar, 161006, People’s Republic of China

    Priti Katrolia, Xiaolan Liu, Guanlong Li & Narasimha Kumar Kopparapu

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  1. Priti Katrolia
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  2. Xiaolan Liu
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  4. Narasimha Kumar Kopparapu
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Correspondence to Xiaolan Liu.

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Katrolia, P., Liu, X., Li, G. et al. Enhanced Properties and Lactose Hydrolysis Efficiencies of Food-Grade β-Galactosidases Immobilized on Various Supports: a Comparative Approach. Appl Biochem Biotechnol 188, 410–423 (2019). https://doi.org/10.1007/s12010-018-2927-8

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