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 9 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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