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Immobilized enzyme

About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.


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Journal ArticleDOI
TL;DR: In conclusion, immobilized beta-glucosidase of Aspergillus phoenicis QM 329 was immobilized on chitosan, using the bifunctional agent glutaraldehyde to exhibit a similar pH optimum but more activity at lower pH values and mass transfer limitations.
Abstract: beta-Glucosidase of Aspergillus phoenicis QM 329 was immobilized on chitosan, using the bifunctional agent glutaraldehyde. The most active preparation based on the amount of support contained a 1:2.5 enzyme-to-chitosan ratio (wt/wt). However, the specific activity of the bound enzyme decreased from 10 to 1% with increasing enzyme-to-chitosan ratio. Compared with free beta-glucosidase, the immobilized enzyme exhibited: (i) a similar pH optimum but more activity at lower pH values; (ii) improved thermal stability; (iii) a similar response to inhibition by glucose; and (iv) mass transfer limitations as reflected by higher apparent Km and lower energy of activation.

126 citations

Journal ArticleDOI
TL;DR: Graphene oxide was synthesized via modified Hummer's method and exploited as an ideal enzyme immobilization support due to its exclusive chemical and structural features and the average decolorization effectiveness of the nanobiocatalyst was more than 75% after six cycles, implies its excellent operational stability and good reusability.

126 citations

Journal ArticleDOI
TL;DR: Polysulfone composite nanofibrous membranes were prepared by electrospinning and were used to immobilize lipase from Candida rugosa by physical adsorption and kinetic parameters of the free and immobilized lipases were higher and lower than those for free lipase, respectively.
Abstract: Polysulfone composite nanofibrous membranes were prepared by electrospinning and were used to immobilize lipase from Candida rugosa by physical adsorption. Field emission scanning electron microscopy was used to evaluate the morphology and diameter of the nanofibers. PVP and PEG were used as additives to render the nanofibrous membranes biocompatibility favored by immobilized enzyme. Effects of post-treatment, additive concentration, pH and temperature were investigated on the adsorption capacity and activity of immobilization preparations, as well as thermal stability. It was found that (1) post-treatment had no significant effect on the adsorption capacity; (2) the increment of PVP or PEG concentration was negative for the adsorption capacity but positive for activity of immobilized lipase; (3) the immobilized lipase showed less sensitivity for pH and higher optimum temperature. Thermal stability for the immobilization preparations was enhanced compared with that for free preparations. The kinetic parameters of the free and immobilized lipases, Km and Vmax were also assayed. Results indicated that Km and Vmax for the immobilized lipases were higher and lower than those for free lipase, respectively.

126 citations

Journal ArticleDOI
TL;DR: In this paper, the feasibility of immobilizing naringinase in a food contact approved packaging film was evaluated and it was shown that the naredinase had an optimum pH of 3.5 and a pH of 4.0 at 7°C.
Abstract: Naringin, a bitter compound in citrus, may be converted to a nonbitter form by enzymic hydrolysis. Our objective was to determine the feasibility of immobilizing naringinase in a food contact approved packaging film. Naringinase from Penicillium sp. was immobilized in cellulose acetate films with up to 23% efficiency at 7°C. Kinetic studies showed that the free enzyme had an optimum pH=3.5 and the immobilized enzyme pH=4.0. Activation energy decreased upon immobilization (from 14.2 to 11.0 Kcal/mol) thus providing an increased catalytic efficiency for immobilized naringinase. The Michaelis constant for immobilized naringinase (K m =2.1 mM) was lower than for free enzyme (K m =3.6 mM). Keeping films under dry storage for 1 moat room temperature did not cause decreased enzyme activity. A film area/volume ratio (cm 2 /mL of 10° Brix grapefruit juice) of 7.2 hydrolyzed 60% of the naringin in 15 days at 7°C.

125 citations

Journal ArticleDOI
TL;DR: This review focuses on the current status of enzyme immobilization, which aims to summarize the latest research on the parameters affecting the performance of immobilized enzyme.
Abstract: Enzyme immobilization has been investigated to improve lipase properties over the past few decades. Different methods and various carriers have been employed to immobilize enzyme. However, the application of enzymatic technology in large scale is rarely seen during the industrial process. The main obstacles are a high cost of the immobilization and the poor performance of immobilized lipase. This review focuses on the current status of enzyme immobilization, which aims to summarize the latest research on the parameters affecting the performance of immobilized enzyme. Particularly, the effect of immobilization methods, immobilization carriers, and enzyme loading has been discussed.

125 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023219
2022417
2021480
2020548
2019553
2018543