• BMB Reports
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• v.44 no.2
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• pp.77-86
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• 2011

Over the years, nanostructures have been developed to enable to support enzyme usability to obtain highly selective and efficient biocatalysts for catalyzing processes under various conditions. This review summarizes recent developments in the nanostructures for enzyme supporters, typically those formed with various inorganic materials. To improve enzyme attachment, the surface of nanomaterials is properly modified to express specific functional groups. Various materials and nanostructures can be applied to improve both enzyme activity and stability. The merits of the incorporation of enzymes in inorganic nanomaterials and unprecedented opportunities for enhanced enzyme properties are discussed. Finally, the limitations encountered with nanomaterial-based enzyme immobilization are discussed together with the future prospects of such systems.

• International Journal of Industrial Entomology and Biomaterials
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• v.27 no.2
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• pp.322-325
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• 2013

In the present study, we report that the selection of operation mode is important to take the full advantage of nanofibrous membrane in enzyme immobilization. Silk fibroin nanofibrous membrane has been prepared by electrospinning, and a-chymotrypsin was immobilized as a model enzyme. When the immobilized enzyme was operated in the membrane reactor mode, the Michaelis constant, Km, was lower and the Vmax was higher compared to the batch reactor mode. No concentration gradient was observed in the membrane reactor mode and the immobilized enzyme was stable even after 7 times of re-use. Our results suggests that the enzyme immobilized nanofibrous membrane should be operated in the membrane reactor mode rather than in the bath reactor mode.

• Bulletin of the Korean Chemical Society
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• v.34 no.9
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• pp.2741-2746
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• 2013

The immobilization of enzyme is one of the key issues both in the field of enzymatic research and industrialization. In this work, we reported a facile method to immobilize Candida Antarctica lipase B (CALB) in alginate carrier. In the presence of calcium cation, the enzyme-alginate suspension could be cross-linked to form beads with porous structure at room temperature, and the enzyme CALB was dispersed in the beads. Activity of the enzyme-alginate composite was verified by enzymatic hydrolysis reaction of p-nitrophenol butyrate in aqueous phase. The effects of reaction parameters such as temperature, pH, embedding and lyophilized time on the reactive behavior were discussed. Reuse cycle experiments for the hydrolysis of p-nitrophenol butyrate demonstrated that activity of the enzyme-alginate composite was maintained without marked deactivation up to 6 repeated cycles.

• Korean Journal of Food Science and Technology
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• v.20 no.4
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• pp.541-546
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• 1988

Optimum conditions for immobilization of aminoacylase on chitosan were investigated, and the results are summerized as follows: Optimum conditions for activation of chitosan were pH 6.0, 0.2% of glutaraldehyde, and 120 minutes of reaction time. Enzyme concentration and reaction time for immobilization of aminoacylase on the activated chitosan were 80mg/20ml, and 90 minutes, respectively, and the yield of activity of the immobilized enzyme was 42.6%.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.1
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• pp.83-87
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• 1999

Immobilization of amyloglucosidase (AMG) with chitosan microbead and its possible applications were evaluated. The diameter of chitosan inicrobead was about 1.2 mm and the optimum enzyme concentration for immobilization was 6 mg/ml. The relative activity of the immobilized enzyme was $97.8\%$ at pH 4.2 and $55^{\circ}C$ and the optimum condition for the immobilized enwme was the same to that of free enzyme. In case of temperature above $30^{\circ}C$, the activity of the immobilized enzyme was a little higher than that of free enzyme. The enzyme activities of both free and immobilized were stable for 6 months when stored at $35^{\circ}C$. The optimum temperatures of both enzymes for saccharification of the dextrinized starch were $55^{\circ}C$ while the relative activity of the immobilized enzlme was $62.6\%$.

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.166-173
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• 1985

Several enzyme immobilization methods has been compared for immobilization of pepsin. Carboxymethyl cellulose and diethylaminoethyl cellulose were activated with Hcl and with NaOH, and were used for immobilization of pepsin. Sepharose-4B was activated cyanogen bromide, and was used for immobilization of pepsin. Porous glass beads were derivatized with 3-aminopropyitrlethoxysilane and with succinicanhydride, and were used for immobilization of pepsin. The results abtained were summarized as follow, 1. 10 mg/gr. dry bead and 15mg/gr. dry bead of pepsin were absorbed to CM-cellulose and DEAE-cellulose, 20 mg/gr. dry bead and 27 mg/gr. dry bead were coupled to CM-cellulose and DEAE-cellulose with glutaraldehyde respectively. Enzyme yields were 22% and 24% of soluble pepsin. 2. 16 mg/gr. dry bead of pepsin was attached to cyanogen bromide activated sepharose-4B, 19mg/gr. dry bead was cross linked to the activated bead with glutaraldehyde. Immobilized enzyme activity was 23% of soluble pepsin. 3. 40 mg/gr. dry bead of pepsin was conjugated to the derivatized glass beads. Immobilized enzyme activity was 45% of soluble pepsin.

• Journal of Microbiology and Biotechnology
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• v.25 no.12
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• pp.2016-2023
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• 2015

Xylanase plays important roles in a broad range of industrial production as a biocatalyst, and its applications commonly require immobilization on supports to enhance its stability. Aluminum hydroxide, a carrier material with high surface area, has the advantages of simple and low-cost preparation and resistance to biodegradation, and can be potentially used as a proper support for xylanase immobilization. In this work, xylanase from Thermomyces lanuginosus was immobilized on two types of aluminum hydroxide particles (gibbsite and amorphous Al(OH)₃) through adsorption, and the properties of the adsorbed enzymes were studied. Both particles had considerable adsorptive capacity and affinity for xylanase. Xylanase retained 75% and 64% of the original catalytic activities after adsorption to gibbsite and amorphous Al(OH)₃. Both the adsorptions improved pH and thermal stability, lowered activation energy, and extended lifespan of the immobilized enzyme, as compared with the free enzyme. Xylanase adsorbed on gibbsite and amorphous Al(OH)₃ retained 71% and 64% of its initial activity, respectively, after being recycled five times. These results indicated that aluminum hydroxides served as good supports for xylanase immobilization. Therefore, the adsorption of xylanase on aluminum hydroxide particles has promising potential for practical production.

• Asian-Australasian Journal of Animal Sciences
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• v.26 no.4
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• pp.552-557
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• 2013

Partially purified ${\alpha}$-galactosidase from Bacillus sp. LX-1 was non-covalently immobilized on a reversibly soluble-insoluble polymer, Eudragit L-100, and an immobilization efficiency of 0.93 was obtained. The optimum pH of the free and immobilized enzyme was 6.5 to 7.0 and 7.0, respectively, while there was no change in optimum temperature between the free and immobilized ${\alpha}$-galactosidase. The immobilized ${\alpha}$-galactosidase was reutilized six times without significant loss in activity. The immobilized enzyme showed good storage stability at $37^{\circ}C$, retaining about 50% of its initial activity even after 18 d at this temperature, while the free enzyme was completely inactivated. The immobilization of ${\alpha}$-galactosidase from Bacillus sp. LX-1 on Eudragit L-100 may be a promising strategy for removal of ${\alpha}$-galacto-oligosaccharides such as raffinose and stachyose from soybean meal and other legume in feed industry.

• Bulletin of the Korean Chemical Society
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• v.33 no.7
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• pp.2181-2186
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• 2012

Dendrimers are a novel class of nonlinear polymers and due to their extensive applications in different fields, called versatile polymers. Polyamidoamine (PAMAM) dendrimers are one of the most important dendrimers that have many applications in nanobiotechnology and industry. Generally aldehyde terminated dendrimers are prepared by activation of amine terminated dendrimers by glutaraldehyde which has two problems, toxicity and possibility of crosslink formation. In this study, novel aldehyde-terminated PAMAM dendrimer was prepared and used for covalent immobilization of trypsin by the aim of finding a special reagent which can prevent crosslinking and deactivation of the enzyme. For this purpose aminoacetaldehydedimethylacetal (AADA) was used as spacer group between aldehyde-terminated PAMAM and trypsin.The findings of this study showed that immobilization of trypsin not only resulted higher optimal temperature, but also increased the thermal stability of the immobilized enzyme in comparison to the free enzyme.

• Bulletin of the Korean Chemical Society
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• v.33 no.10
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• pp.3458-3460
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• 2012