The Experts below are selected from a list of 22416 Experts worldwide ranked by ideXlab platform
Chwen-jen Shieh - One of the best experts on this subject based on the ideXlab platform.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly gamma glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Shuofen Chang, Jeifu Shaw, Kairuei Yang, Chwen-jen ShiehAbstract:Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly γ glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Jeifu Shaw, K H Yang, S F Chang, Chwen-jen ShiehAbstract:Poly(γ-glutamic acid) (γ-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on γ-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2–6 h), immobilization temperature (0–26 °C), and enzyme/support ratio (0.1–0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3 h, immobilization temperature 13.3 °C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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optimum immobilization of candida rugosa lipase on celite by rsm
Applied Clay Science, 2007Co-Authors: Shuofen Chang, Shu-wei Chang, Yuehorng Yen, Chwen-jen ShiehAbstract:Abstract Immobilization of Candida rugosa lipase (lipase AY-30) by adsorption on Celite led to a markedly improved performance of the enzyme. Immobilization conditions and characterization of the immobilized enzyme were investigated. Lipase activity was measured with glycerol tributyrate as substrate. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (30–90 min), immobilization temperature (0–20 °C), and enzyme/support ratio (0.3–0.5, w/w), on the specific activity of immobilized lipase. Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 59.1 min, immobilization temperature 10.7 °C, and enzyme/support ratio 0.5 (w/w); the highest specific activity obtained was 18.16 U/mg-protein with activity yield of 34.1%.
Shu-wei Chang - One of the best experts on this subject based on the ideXlab platform.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly gamma glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Shuofen Chang, Jeifu Shaw, Kairuei Yang, Chwen-jen ShiehAbstract:Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly γ glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Jeifu Shaw, K H Yang, S F Chang, Chwen-jen ShiehAbstract:Poly(γ-glutamic acid) (γ-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on γ-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2–6 h), immobilization temperature (0–26 °C), and enzyme/support ratio (0.1–0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3 h, immobilization temperature 13.3 °C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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optimum immobilization of candida rugosa lipase on celite by rsm
Applied Clay Science, 2007Co-Authors: Shuofen Chang, Shu-wei Chang, Yuehorng Yen, Chwen-jen ShiehAbstract:Abstract Immobilization of Candida rugosa lipase (lipase AY-30) by adsorption on Celite led to a markedly improved performance of the enzyme. Immobilization conditions and characterization of the immobilized enzyme were investigated. Lipase activity was measured with glycerol tributyrate as substrate. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (30–90 min), immobilization temperature (0–20 °C), and enzyme/support ratio (0.3–0.5, w/w), on the specific activity of immobilized lipase. Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 59.1 min, immobilization temperature 10.7 °C, and enzyme/support ratio 0.5 (w/w); the highest specific activity obtained was 18.16 U/mg-protein with activity yield of 34.1%.
Shuofen Chang - One of the best experts on this subject based on the ideXlab platform.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly gamma glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Shuofen Chang, Jeifu Shaw, Kairuei Yang, Chwen-jen ShiehAbstract:Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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optimum immobilization of candida rugosa lipase on celite by rsm
Applied Clay Science, 2007Co-Authors: Shuofen Chang, Shu-wei Chang, Yuehorng Yen, Chwen-jen ShiehAbstract:Abstract Immobilization of Candida rugosa lipase (lipase AY-30) by adsorption on Celite led to a markedly improved performance of the enzyme. Immobilization conditions and characterization of the immobilized enzyme were investigated. Lipase activity was measured with glycerol tributyrate as substrate. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (30–90 min), immobilization temperature (0–20 °C), and enzyme/support ratio (0.3–0.5, w/w), on the specific activity of immobilized lipase. Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 59.1 min, immobilization temperature 10.7 °C, and enzyme/support ratio 0.5 (w/w); the highest specific activity obtained was 18.16 U/mg-protein with activity yield of 34.1%.
Edmond Magner - One of the best experts on this subject based on the ideXlab platform.
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rapid in situ immobilization of enzymes in metal organic framework supports under mild conditions
Chemcatchem, 2017Co-Authors: Victoria Gascon, Cristina Carucci, Mayra B Jimenez, Rosa M Blanco, Manuel Sanchezsanchez, Edmond MagnerAbstract:The use of a metal organic framework (MOF) as a support for the in-situ Immobilisation of enzymes is described. The MOF support, a Basolite F300-like material, was prepared from FeCl3 and the tridentate linker trimesic acid. Immobilisation of alcohol dehydrogenase, lipase and glucose oxidase was performed in-situ under mild conditions (aqueous solution, neutral pH and at room temperature) in a rapid and facile manner with retention of activity for at least one week. The catalytic activities of lipase and glucose oxidase were similar to the activities of the free enzymes; with alcohol dehydrogenase, there was a substantial decrease in activity on immobilization that may arise from diffusion limitations. The approach demonstrates that a MOF material, prepared from cheap and commercially available materials, can be successively utilised to prepare stable and catalytically active biocatalysts in a rapid and facile manner.
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understanding enzyme Immobilisation
Chemical Society Reviews, 2009Co-Authors: Ulf Hanefeld, Lucia Gardossi, Edmond MagnerAbstract:Enzymes are versatile catalysts in the laboratory and on an industrial scale. To broaden their applicability in the laboratory and to ensure their (re)use in manufacturing the stability of enzymes can often require improvement. Immobilisation can address the issue of enzymatic instability. Immobilisation can also help to enable the employment of enzymes in different solvents, at extremes of pH and temperature and exceptionally high substrate concentrations. At the same time substrate-specificity, enantioselectivity and reactivity can be modified. However, most often the molecular and physical–chemical bases of these phenomena have not been elucidated yet. This tutorial review focuses on the understanding of enzyme Immobilisation.
Jeifu Shaw - One of the best experts on this subject based on the ideXlab platform.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly γ glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Jeifu Shaw, K H Yang, S F Chang, Chwen-jen ShiehAbstract:Poly(γ-glutamic acid) (γ-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on γ-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2–6 h), immobilization temperature (0–26 °C), and enzyme/support ratio (0.1–0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3 h, immobilization temperature 13.3 °C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
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studies of optimum conditions for covalent immobilization of candida rugosa lipase on poly gamma glutamic acid by rsm
Bioresource Technology, 2008Co-Authors: Shu-wei Chang, Shuofen Chang, Jeifu Shaw, Kairuei Yang, Chwen-jen ShiehAbstract:Poly(gamma-glutamic acid) (gamma-PGA) is a material of polymer. Immobilization of Candida rugosa lipase (Lipase AY-30) by covalent binding on gamma-PGA led to a markedly improved performance of the enzyme. Response surface methodology (RSM) and 3-level-3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (2-6h), immobilization temperature (0-26 degrees C), and enzyme/support ratio (0.1-0.5, w/w). Based on the analysis of ridge max, the optimum immobilization conditions were as follows: immobilization time 2.3h, immobilization temperature 13.3 degrees C, and enzyme/support ratio 0.41 (w/w); the highest lipase activity obtained was 1196 U/mg-protein.
