Immobilization of <i>β</i>‐Galactosidase on Monolithic Discs for the Production of Prebiotics Galacto‐oligosaccharides

Pottratz, Ines; Schmidt, Christian; Müller, Ines; Hamel, Christof

doi:10.1002/cite.202000231

Cited by 2 publications

(2 citation statements)

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“…The comparison of GOS yield vs. lactose conversion obtained with free or immobilized enzyme offered that the reaction has been shifted towards the transgalactosylation due to the increased E/S ratio in the reactor volume and the lack of diffusion limitation in the monolithic immobilized PTFRs (Figure 4b). The higher affinity of the immobilized enzyme towards the desired GOS synthesis than to hydrolysis is comparable with results obtained in [18,34]. The GOS degradation starts at a lactose conversion of 40% with the free enzyme and at a conversion rate of about 57% for the immobilized PTFRs (Figure 4b), which leads to the synthesis of GOS with a higher, favorable degree of polymerization.…”

Section: Continuous and Semi-continuous Configurationsupporting

confidence: 80%

“…Therefore, the characterization of the carrier in respect to the influence of the chemical activation to the enzyme properties, enzyme activity and transgalactosylation rate in the PTFR is crucial. In our previous work [34] β-gal from B. circulans immobilized on aldehyde, ethylendiamin and carbonyldiimidazole (CDI) activated monolithic PTFRs in the form of small scale disks have been studied and compared. The experiments demonstrated that a shift towards the transgalactosylation rate takes place compared to the free enzyme system in a batch reactor is possible.…”

Section: Introductionmentioning

confidence: 99%

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Potential and Scale-Up of Pore-Through-Flow Membrane Reactors for the Production of Prebiotic Galacto-Oligosaccharides with Immobilized β-Galactosidase

2021

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The production of prebiotics like galacto-oligosaccharides (GOS) on industrial scale is becoming more important due to increased demand. GOS are synthesized in batch reactors from bovine lactose using the cost intensive enzyme β-galactosidase (β-gal). Thus, the development of sustainable and more efficient production strategies, like enzyme immobilization in membrane reactors are a promising option. Activated methacrylatic monoliths were characterized as support for covalent immobilized β-gal to produce GOS. The macroporous monoliths act as immobilized pore-through-flow membrane reactors (PTFR) and reduce the influence of mass-transfer limitations by a dominating convective pore flow. Monolithic designs in the form of disks (0.34 mL) and for scale-up cylindric columns (1, 8 and 80 mL) in three different reactor operation configurations (semi-continuous, continuous and continuous with recirculation) were studied experimentally and compared to the free enzyme system. Kinetic data, immobilization efficiency, space-time-yield and long-term stability were determined for the immobilized enzyme. Furthermore, simulation studies were conducted to identify optimal operation conditions for further scale-up. Thus, the GOS yield could be increased by up to 60% in the immobilized PTFRs in semi-continuous operation compared to the free enzyme system. The enzyme activity and long-time stability was studied for more than nine months of intensive use.

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Section: Continuous and Semi-continuous Configurationsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Potential and Scale-Up of Pore-Through-Flow Membrane Reactors for the Production of Prebiotic Galacto-Oligosaccharides with Immobilized β-Galactosidase

2021

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The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

Alzahrani,

Akanbi,

Scarlett

et al. 2024

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The use of edible oils and fats in dairy products is becoming increasingly important in the food industry because of their complementary functional properties. Most of these products are produced using food-grade enzymes as processing aids because processes involving enzymes are considered mild and environmentally friendly for regulatory purposes. The poor stability and recovery of enzymes in their native state limit their performance, and to enhance their activity, stability, and reusability, enzymes are often immobilised—a process that involves attaching them to a solid support. Additionally, immobilisation enables enzymes to selectively target specific substrates or products, making them highly efficient. These features have led to the increased use of immobilised enzymes in dairy and lipid processing and enzymes have been used to produce a broad range of products such as whey protein concentrates and isolates, peptide–lipid conjugates, lipid concentrates, structured lipids, and human milk fat substitutes. Therefore, this article reviews the current progress on different enzyme preparations and their use in lipid and dairy processing. It also summarises opportunities in enzyme-catalysed valorisation of dairy and lipid waste streams with the ultimate goals of sustainable food production and reductions in waste.

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Immobilization of β‐Galactosidase on Monolithic Discs for the Production of Prebiotics Galacto‐oligosaccharides

Cited by 2 publications

References 16 publications

Potential and Scale-Up of Pore-Through-Flow Membrane Reactors for the Production of Prebiotic Galacto-Oligosaccharides with Immobilized β-Galactosidase

Potential and Scale-Up of Pore-Through-Flow Membrane Reactors for the Production of Prebiotic Galacto-Oligosaccharides with Immobilized β-Galactosidase

The Use of Immobilised Enzymes for Lipid and Dairy Processing and Their Waste Products: A Review of Current Progress

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