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


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.


β-Galactosidase Immobilization Lactose hydrolysis Chitosan Alginate Food grade 


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.


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© 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

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