Purified lactases versus whole-cell lactases-the winner takes it all

Robin Dorau, Peter Ruhdal Jensen, Christian Solem*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review


Lactose-free dairy products are in great demand worldwide due to the high prevalence of lactose intolerance. To make lactose-free dairy products, commercially available β-galactosidase enzymes, also termed lactases, are used to break down lactose to its constituent monosaccharides, glucose and galactose. In this mini-review, the characteristics of lactase enzymes, their origin, and ways of use are discussed in light of their potential for hydrolyzing lactose. We also discuss whole-cell lactase catalysts, which appear to have great potential in terms of cost reduction and convenience, and which are more natural alternatives to purified enzymes. Lactic acid bacteria (LAB) already used in food fermentations seem to be optimal candidates for whole-cell lactases. However, they have not been industrially exploited yet due to technical hurdles. For whole-cell lactases to be efficient, the lactase enzymes inside the cells must be made available for lactose hydrolysis, and thus, cells need to be permeabilized or disrupted prior to use. Here we review state-of-the-art approaches for disrupting or permeabilizing microorganisms. Lastly, based on recent scientific achievements, we propose a novel, resource-efficient, and low-cost scenario for achieving lactose hydrolysis at a dairy plant using a LAB whole-cell lactase.Key points• Lactases (β-galactosidase) are essential for producing lactose-free dairy products• Novel permeabilization techniques facilitate the use of LAB lactases• Whole-cell lactase catalysts have great potential for reducing costs and resources Graphical abstract.
Original languageEnglish
JournalApplied Microbiology and Biotechnology
Pages (from-to)4943–4955
Publication statusPublished - 2021


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