Refolding of D-hydantoinase with fed-batch dilution process
碩士 === 國立中興大學 === 化學工程學系所 === 94 === Recombinant D-hydantoinase was over-expressed in Escherichia coli in the form of inclusion bodies, which contained large amount of the targeted proteins are valuable for industrial application if these protein could be reforded. An optimal refolding procedure has...
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| Format: | Others |
| Language: | zh-TW |
| Published: |
2006
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| Online Access: | http://ndltd.ncl.edu.tw/handle/18524253638237205364 |
| Summary: | 碩士 === 國立中興大學 === 化學工程學系所 === 94 === Recombinant D-hydantoinase was over-expressed in Escherichia coli in the form of inclusion bodies, which contained large amount of the targeted proteins are valuable for industrial application if these protein could be reforded. An optimal refolding procedure has been developed to reford active proteins from inclusion bodies. The inclusion bodies were solubilized in 50mM Tris-buffer at pH 12.5 and then were diluted to refold the denatured proteins. Refolding of D-hydantoinase by direct and fed-batch operations was investigated . Furthermore, the influence of the additives, CTAB and MnCl2, for soluble protein recovery was also studied. The results of the experiments indicate that refolding process with low velocity in the fed-batch operation resulted in higher recovery of soluble protein and it is not recommended to add additives for refolding procedure.
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