Enhanced Properties and Lactose Hydrolysis Efficiencies of Food-Grade β-Galactosidases Immobilized on Various Supports: a Comparative Approach
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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.
Keywordsβ-Galactosidase Immobilization Lactose hydrolysis Chitosan Alginate Food grade
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.
- 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.Bosso, A., Morioka, L. R. I., dos Santos, L. F., & Suguimoto, H. H. (2016). Lactose hydrolysis potential and thermal stability of commercial &#946;-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
- 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.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.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.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.
- 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
- 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
- 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
- 27.Norouzian D.. (2003). Enzyme immobilization: The state of art in biotechnology. Iranian Journal of Biotechnology, 1(4).Google Scholar
- 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