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

Dorau, Robin; Jensen, Peter Ruhdal; Solem, Christian

doi:10.1007/s00253-021-11388-7

Cited by 6 publications

(2 citation statements)

References 96 publications

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“…Apart from immobilized beta-galactosidases, whole cells as such or immobilised by surface display technology have been used as biocatalysts. 183,184 An important prebiotic called lactulose is just a disaccharide of galactose and fructose and has been produced using beta-galactosidase, both in free and immobilised forms. Apart from its use as a prebiotic, it has been used to improve sensory characteristics of food products.…”

Section: Whey As a Biomass: A Classical But Ongoing Story In Waste Va...mentioning

confidence: 99%

White & grey biotechnologies for shaping a sustainable future

Roy¹,

Gupta²

2023

RSC Sustain.

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Section: Whey As a Biomass: A Classical But Ongoing Story In Waste Va...mentioning

confidence: 99%

White & grey biotechnologies for shaping a sustainable future

Roy¹,

Gupta²

2023

RSC Sustain.

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“…For instance, at pH of 4.5 about 45% of the optimum activity is retained. This property makes RBBL a promising option to remove lactose from acidic dairy products (Dorau et al, 2021).…”

Section: Ph Effectsmentioning

confidence: 99%

Lactose hydrolysis in milk using a commercial recombinant β-galactosidase (lactase) from Bifidobacterium bifidum

2022

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We have identified the most relevant properties of a commercial recombinant lactase from Bifidobacterium bifidum (RBBL, Saphera 2600 L) for milk hydrolysis, with a yeast neutral lactase (GODO-YNL2) being used for comparison. Both products were characterized according to their lactase and invertase activities, protein profiles by sodium-dodecyl-sulfate-polyacrylamidegel electrophoresis, and Kms for lactose. RBBL exhibited properties that permitted milk hydrolysis over a broader range of conditions than YNL: apparently, milk's ionic composition was not an activity-limiting property, an optimum temperature range between 45 and 50 °C and a considerable activity at pH 4.5, which would permit lactose hydrolysis in acidic dairy products. Like YNL, the bacterial lactase retains a considerable activity under refrigeration (3-7 °C). To describe the lactose-hydrolysis time course, an empirical model was used in which the glucose obtained was expressed as a function of the standard activity per unit volume and the reaction time. This model proved adequate to describe the glucose-formation kinetics at 7 °C and 45 °C, up to a 95% hydrolysis and to facilitate calculation of the volumen-based enzyme dosage to obtain a certain degree of hydrolysis -a fundamental consideration in evaluating the costs of applying the enzyme

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Synthesis of Galacto-oligosaccharides in Milk by Using Bifidobacterium bifidum β-galactosidases (Saphera 2600L and Nola Fit 5500) Immobilized on Chitosan Beads

Bodnár,

Fazekas,

Nagy

et al. 2023

Food Bioprocess Technol

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The lactose intolerance—as a limiting factor for dairy milk consumption—has a high prevalence worldwide. Dairy milk and milk-derived products are major sources of multiple inorganic compounds and nutrients and thus are considered to be functional foods. β-galactosidases are able to hydrolyze lactose and are therefore widely applied for the production of lactose-free products. In addition, they are capable of the synthesis of galacto-oligosaccharides (GOSs); thus, the dairy industry has a special interest in applying them for the enrichment of dairy products with prebiotic GOSs. In this work, we studied two commercially available β-galactosidase products: Saphera 2600L and Nola Fit 5500. Both enzyme solutions contain a recombinant β-galactosidase of Bifidobacterium bifidum and have already been authorized for food industrial application, but the information about their hydrolytic and/or synthetic activities is only limited. After immobilization on chitosan beads, the enzymes were used for lactose hydrolysis and simultaneous synthesis of GOSs, by performing the reactions in pasteurized milk (skim milk). Both immobilized β-galactosidase exhibited elevated lactose hydrolysis (vmax increased from ~ 1 to ~ 4 mM/min) and GOS synthesis as compared to the free enzymes. The enzyme-coated beads were efficiently re-used at least 15 cycles; the residual lactose concentration was < 2 mg/ml after each cycle. After treatment, GOSs were present in ≤ 9% of the total sugar content, indicating that the prepared low-lactose milks were enriched in prebiotic GOSs. The application of immobilized Saphera 2600L and Nola Fit 5500 β-galactosidases may be implemented for the large-scale production of GOS-enriched low-lactose milk. Graphical Abstract

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

Cited by 6 publications

References 96 publications

White & grey biotechnologies for shaping a sustainable future

White & grey biotechnologies for shaping a sustainable future

Lactose hydrolysis in milk using a commercial recombinant β-galactosidase (lactase) from Bifidobacterium bifidum

Synthesis of Galacto-oligosaccharides in Milk by Using Bifidobacterium bifidum β-galactosidases (Saphera 2600L and Nola Fit 5500) Immobilized on Chitosan Beads

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