Immobilization of β-Galactosidase in Adsorptive Membranes for the Continuous Production of Galacto-Oligosaccharides from Lactose

Engel, L. David; Schneider, Philipp; Ebrahimi, Mehrdad; Czermak, Peter

doi:10.2174/187425640701011704

Cited by 6 publications

(7 citation statements)

References 4 publications

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“…This could be partially solved by using immobilised enzymes, but it was finally Engel et al, who showed that the amendment of a membrane separation technique, together with enzyme immobilisation improved the purity and production process significantly. 237,238 Das et al and Sen et al showed that GOS can be produced from lactose with a membrane-immobilised enzyme. 78,239 The required enzyme, a b-galactosidase, was immobilised on a poly(ethersulphone) ultrafiltration membrane using polyethyleneimine, 240 an extremely branched cationic chain polymer, 241 for use in a rotating disk membrane reactor (RDMBR).…”

Section: Production Of Carbohydrate-based Renewables For Pharma and Fmentioning

confidence: 99%

Immobilised enzymes in biorenewables production

et al. 2013

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Oils, fats, carbohydrates, lignin, and amino acids are all important raw materials for the production of biorenewables. These compounds already play an important role in everyday life in the form of wood, fabrics, starch, paper and rubber. Enzymatic reactions do, in principle, allow the transformation of these raw materials into biorenewables under mild and sustainable conditions. There are a few examples of processes using immobilised enzymes that are already applied on an industrial scale, such as the production of High-Fructose Corn Syrup, but these are still rather rare. Fortunately, there is a rapid expansion in the research efforts that try to improve this, driven by a combination of economic and ecological reasons. This review focusses on those efforts, by looking at attempts to use fatty acids, carbohydrates, proteins and lignin (and their building blocks), as substrates in the synthesis of biorenewables using immobilised enzymes. Therefore, many examples (390 references) from the recent literature are discussed, in which we look both at the specific reactions as well as to the methods of immobilisation of the enzymes, as the latter are shown to be a crucial factor with respect to stability and reuse. The applications of the renewables produced in this way range from building blocks for the pharmaceutical and polymer industry, transport fuels, to additives for the food industry. A critical evaluation of the relevant factors that need to be improved for large-scale use of these examples is presented in the outlook of this review.

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Section: Production Of Carbohydrate-based Renewables For Pharma and Fmentioning

confidence: 99%

Immobilised enzymes in biorenewables production

et al. 2013

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“…During enzymatic hydrolysis of lactose into glucose and galactose, using β‐galactosidases, the enzyme is also able to transfer galactose to the hydroxyl groups of galactose or glucose in a process called “transgalactosylation” and, thus, produces GOS . GOS are nondigestible oligosaccharides which are recognized as prebiotics, thus stimulating the growth of bifidobacteria in the lower part of the human intestine …”

Section: Introductionmentioning

confidence: 99%

Covalent Immobilization of β‐Galactosidase onto Amino‐Functionalized Polyvinyl Chloride Microspheres: Enzyme Immobilization and Characterization

et al. 2013

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ABSTRACT:In this study, β-galactosidase (Aspergillus oryzae) was covalently immobilized onto aminated polyvinyl chloride (PVC) via glutaraldehyde coupling. Effect of immobilization conditions was investigated. The maximum obtained immobilization yield is 27 units g −1 while the maximum expressed activity is 12 μmol minThe optimum pH of the free enzyme was observed at 5.2, whereas the optimum pH of the immobilized one was schiffed to 4.4. The optimum temperature for both the free and immobilized forms was recognized at 60• C. A change in the temperature profile of the immobilized enzyme below 60• C was observed when response to the elevation temperature was less than that to the free counterpart. The K m and V max values of the free and immobilized β-galactosidase were found to be 52.03 and 123.1 mM, and 6.12 and 9.98 μ mol/min, respectively. Lactose hydrolysis, 500 mL of 100 mM concentration, was studied using 400 units of either free or immobilized enzymes at pH 6.0 and 60• C. Almost 80% hydrolysis percentage has been obtained after 6 h hydrolysis time with immobilized enzyme compared with 63% hydrolysis percentage obtained after 2 h for the free counterpart. Investigation of the operational stability at 40• C shows that the immobilized enzyme kept its activity for 5 h over 10 successive lactose hydrolysis cycles, which provides potentials for practical application in milk and whey hydrolysis. C

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“…Some study has applied external pressure to improve enzyme adsorption into the pores on the surface and also within the membrane through ultrafiltration. 9,26,27 However, enzyme immobilized into the pores within the membrane matrixes yielded lower specific productivity due to substrate diffusion limitation. 8 Hence, intensifying the occupation of enzyme-bounded on the membrane surface via PEI is preferred where the enzymatic layer is easily in contact with the bulk substrate solution.…”

Section: Resultsmentioning

confidence: 99%

Simultaneous Adsorption and Fixation of Aspergillus oryzae β-Galactosidase on Polyelectrolyte-Layered Polysulfone Hollow-Fiber Membrane

Gonawan

Kamaruddin

Bakar

et al. 2015

Ind. Eng. Chem. Res.

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A simple procedure involving simultaneous adsorption and fixation was developed to immobilize β-galactosidase (β-Gal) from Aspergillus oryzae on a polysulfone hollow-fiber membrane module for converting lactose to galactooligosaccharides. Polyethylenimine was used as a polyelectrolyte intermediate layer to provide a positively charged character for β-Gal adsorption. β-Gal adsorbed on polyethylenimine layer was then fixed with cross-linking by glutaraldehyde. The concentrations of polyethylenimine, glutaraldehyde, and β-Gal were significant parameters to achieve high activity yield. The optimum concentration of polyethylenimine and glutaraldehyde were determined as 5% (w/v) and 15% (v/v), respectively. The activity yield on the membrane surface increases as the concentration of β-Gal used during adsorption and fixation increased. The highest activity yield obtained was 1.26 IU cm −2 at 5 mg mL −1 of β-Gal concentration. The activity yield is proportionally dependent on the concentration of the β-Gal employed. Moreover, the immobilized β-Gal exhibited higher specific productivity and stable transgalactosylation activity compared with free β-Gal during the lactose-catalyzed conversion reaction.

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Immobilization of β-Galactosidase in Adsorptive Membranes for the Continuous Production of Galacto-Oligosaccharides from Lactose

Cited by 6 publications

References 4 publications

Immobilised enzymes in biorenewables production

Immobilised enzymes in biorenewables production

Covalent Immobilization of β‐Galactosidase onto Amino‐Functionalized Polyvinyl Chloride Microspheres: Enzyme Immobilization and Characterization

Simultaneous Adsorption and Fixation of Aspergillus oryzae β-Galactosidase on Polyelectrolyte-Layered Polysulfone Hollow-Fiber Membrane

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