Immobilization of Aspergillus oryzae β-galactosidase on low-pressure plasma-modified cellulose acetate membrane using polyethyleneimine for production of galactooligosaccharide

Güleç, Hacı Ali; Gürdaş, Sevim; Albayrak, Nedim; Mutlu, Mehmet

doi:10.1007/s12257-010-0046-7

Cited by 30 publications

(12 citation statements)

References 27 publications

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“…Later, a similar protocol was used using as support low-pressure plasma-modified cellulose acetate membrane. 252 Lactase was also covalently attached to low-density polyethylene for in-package production of lactose-free dairy products. 253 Multilayers of the enzyme were immobilized alternating polyethylenimine, glutaraldehyde and lactase (the 5-layer sample reaching up to 1.3 µg lactase/cm 2 ), although the affinity of the immobilized lactase towards the substrate remains unchanged after immobilization, the k cat showed a decrease with each layer of attached lactase.…”

Section: Journal Of Materials Chemistry B Accepted Manuscriptmentioning

confidence: 99%

Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts

et al. 2017

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Section: Journal Of Materials Chemistry B Accepted Manuscriptmentioning

confidence: 99%

Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts

et al. 2017

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“…Enzymatic activity evolution was represented by the classical Michaelis-Menten Equation (1) [13,22] and is represented in Figure 3. Then, kinetics parameters were determined using the LineweaverBurk representation for the immobilized and free enzyme (Figure 3 A decrease of only 40% of the enzymatic activity was observed after three runs, followed by good stability in the subsequent runs.…”

Section: Kinetic Parameters Of Immobilized β-Galmentioning

confidence: 99%

Investigation of the Effect of Plasma Polymerized Siloxane Coating for Enzyme Immobilization and Microfluidic Device Conception

et al. 2016

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This paper describes the impact of a physical immobilization methodology, using plasma polymerized 1,1,3,3, tetramethyldisiloxane, on the catalytic performance of β-galactosidase from Aspergillus oryzae in a microfluidic device. The β-galactosidase was immobilized by a polymer coating grown by Plasma Enhanced Chemical Vapor Deposition (PEVCD). Combined with a microchannel patterned in the silicone, a microreactor was obtained with which the diffusion through the plasma polymerized layer and the hydrolysis of a synthetic substrate, the resorufin-β-D-galactopyranoside, were studied. A study of the efficiency of the immobilization procedure was investigated after several uses and kinetic parameters of immobilized β-galactosidase were calculated and compared with those of soluble enzyme. Simulation and a modelling approach were also initiated to understand phenomena that influenced enzyme behavior in the physical immobilization method. Thus, the catalytic performances of immobilized enzymes were directly influenced by immobilization conditions and particularly by the diffusion behavior and availability of substrate molecules in the enzyme microenvironment.

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“…The immobilized biocatalyst enabled the GOS production of 26% ( w / w ) of total sugars, from a feed lactose solution of 40% ( w / v ) lactose at pH 4.5 and 40 °C, at 50% lactose conversion. The production of GOS from lactose was also carried out using β-galactosidase from Aspergillus oryzae, immobilized on a low-pressure plasma-modified cellulose acetate [129]. The novel method developed for multilayer enzyme immobilization involved the formation of a polyethyleneimine (PEI)-enzyme aggregate and concomitant growth on a cellulose acetate membrane.…”

Section: Immobilized Carbohydrases In the Production Of Prebioticsmentioning

confidence: 99%

Potential Applications of Carbohydrases Immobilization in the Food Industry

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Kawaguti

et al. 2013

IJMS

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Carbohydrases find a wide application in industrial processes and products, mainly in the food industry. With these enzymes, it is possible to obtain different types of sugar syrups (viz. glucose, fructose and inverted sugar syrups), prebiotics (viz. galactooligossacharides and fructooligossacharides) and isomaltulose, which is an interesting sweetener substitute for sucrose to improve the sensory properties of juices and wines and to reduce lactose in milk. The most important carbohydrases to accomplish these goals are of microbial origin and include amylases (α-amylases and glucoamylases), invertases, inulinases, galactosidases, glucosidases, fructosyltransferases, pectinases and glucosyltransferases. Yet, for all these processes to be cost-effective for industrial application, a very efficient, simple and cheap immobilization technique is required. Immobilization techniques can involve adsorption, entrapment or covalent bonding of the enzyme into an insoluble support, or carrier-free methods, usually based on the formation of cross-linked enzyme aggregates (CLEAs). They include a broad variety of supports, such as magnetic materials, gums, gels, synthetic polymers and ionic resins. All these techniques present advantages and disadvantages and several parameters must be considered. In this work, the most recent and important studies on the immobilization of carbohydrases with potential application in the food industry are reviewed.

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Immobilization of Aspergillus oryzae β-galactosidase on low-pressure plasma-modified cellulose acetate membrane using polyethyleneimine for production of galactooligosaccharide

Cited by 30 publications

References 27 publications

Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts

Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts

Investigation of the Effect of Plasma Polymerized Siloxane Coating for Enzyme Immobilization and Microfluidic Device Conception

Potential Applications of Carbohydrases Immobilization in the Food Industry

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