Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748

碩士 === 元智大學 === 化學工程與材料科學學系 === 96 === In this study, the application of chelating resin Amberlite IRC-748 as ion-exchange absorbent for separation of bovine serum albumin ( BSA ) and bovine hemoglobin ( BHb ) mixture. The effects of pH, temperature and salt concentration on single protein adsorptio...

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Main Authors: Hsiao-Chiao Weng, 翁小喬
Other Authors: 莊瑞鑫
Format: Others
Language:zh-TW
Published: 2008
Online Access:http://ndltd.ncl.edu.tw/handle/16849806743348530884
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spelling ndltd-TW-096YZU051590012015-10-13T13:48:20Z http://ndltd.ncl.edu.tw/handle/16849806743348530884 Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748 以螯合樹脂AmberliteIRC-748分離牛血紅素與牛血清蛋白混合物 Hsiao-Chiao Weng 翁小喬 碩士 元智大學 化學工程與材料科學學系 96 In this study, the application of chelating resin Amberlite IRC-748 as ion-exchange absorbent for separation of bovine serum albumin ( BSA ) and bovine hemoglobin ( BHb ) mixture. The effects of pH, temperature and salt concentration on single protein adsorption and thermodynamics were investigated. Furthermore, separation factor and the kinetics properties of binary protein system were also investigated with adsorption process. Finally, it was discussed with desorption conditions. For both proteins, amount of adsorption was higher at low pH values. The results show that the amount of protein adsorbed increases as the temperature and salt concentration increase. In addition, the adsorption isotherms well fitted by the Langmuir isothermal model from the semi-reciprocal plot analysis. Utilizing Van’t Hoff relationships to analyze the experimental data for these interactions, the change in the apparent enthalpy of association for the adsorption of BSA and BHb onto IRC-748 was positive. In binary protein adsorption experiment, it could be separated completely at 40oC, pH 4.0 with 0.2 M NaCl. However, the condition at 40oC, pH 5.0 with 0.2 M NaCl showed the best adsorption selectivity. It has shown that adsorption behavior with competitive phenomenon when using the three competitive adsorption models in binary component system. In order to investigate the mechanism of adsorption and potential rate controlling step, first- and second-order kinetic equations, intraparticle diffusion model and external film mass transfer model have been used for testing experimental data. Adsorption of both proteins is best fit by second-order kinetic equation. In these adsorption conditions, the adsorption mechanism of BSA is external film diffusion controlling and BHb can be best described by intraparticle diffusion model. Aspect to desorption experiment, by using modified pH value will find that the desorption percentage of protein which adsorb at low temperature will better than high temperature. 莊瑞鑫 2008 學位論文 ; thesis 105 zh-TW
collection NDLTD
language zh-TW
format Others
sources NDLTD
description 碩士 === 元智大學 === 化學工程與材料科學學系 === 96 === In this study, the application of chelating resin Amberlite IRC-748 as ion-exchange absorbent for separation of bovine serum albumin ( BSA ) and bovine hemoglobin ( BHb ) mixture. The effects of pH, temperature and salt concentration on single protein adsorption and thermodynamics were investigated. Furthermore, separation factor and the kinetics properties of binary protein system were also investigated with adsorption process. Finally, it was discussed with desorption conditions. For both proteins, amount of adsorption was higher at low pH values. The results show that the amount of protein adsorbed increases as the temperature and salt concentration increase. In addition, the adsorption isotherms well fitted by the Langmuir isothermal model from the semi-reciprocal plot analysis. Utilizing Van’t Hoff relationships to analyze the experimental data for these interactions, the change in the apparent enthalpy of association for the adsorption of BSA and BHb onto IRC-748 was positive. In binary protein adsorption experiment, it could be separated completely at 40oC, pH 4.0 with 0.2 M NaCl. However, the condition at 40oC, pH 5.0 with 0.2 M NaCl showed the best adsorption selectivity. It has shown that adsorption behavior with competitive phenomenon when using the three competitive adsorption models in binary component system. In order to investigate the mechanism of adsorption and potential rate controlling step, first- and second-order kinetic equations, intraparticle diffusion model and external film mass transfer model have been used for testing experimental data. Adsorption of both proteins is best fit by second-order kinetic equation. In these adsorption conditions, the adsorption mechanism of BSA is external film diffusion controlling and BHb can be best described by intraparticle diffusion model. Aspect to desorption experiment, by using modified pH value will find that the desorption percentage of protein which adsorb at low temperature will better than high temperature.
author2 莊瑞鑫
author_facet 莊瑞鑫
Hsiao-Chiao Weng
翁小喬
author Hsiao-Chiao Weng
翁小喬
spellingShingle Hsiao-Chiao Weng
翁小喬
Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
author_sort Hsiao-Chiao Weng
title Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
title_short Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
title_full Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
title_fullStr Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
title_full_unstemmed Separation of Bovine Serum Albumin ( BSA ) and Bovine Hemoglobin ( BHb ) Mixtures with a Chelating Resin Amberlite IRC-748
title_sort separation of bovine serum albumin ( bsa ) and bovine hemoglobin ( bhb ) mixtures with a chelating resin amberlite irc-748
publishDate 2008
url http://ndltd.ncl.edu.tw/handle/16849806743348530884
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