tailieunhanh - Báo cáo khoa học: Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase

In vitrorefolding of maltodextrin glucosidase, a 69 kDa monomericEscher-ichia coli protein, was studied in the presence of glycerol, dimethylsulfox-ide, trimethylamine-N-oxide, ethylene glycol, trehalose, proline and chaperonins GroEL and GroES. | ễFEBS Journal Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase Subhankar Paul1 2 Shashikala Punam1 and Tapan K. Chaudhuri1 1 Department of BiochemicalEngineering and Biotechnology Indian Institute of Technology Delhi India 2 Department of Biotechnology and MedicalEngineering NationalInstitute of Technology Rourkela India Keywords chemical chaperone-assisted refolding GroEL GroES MalZ protein aggregation Correspondence S. Paul Department of Biotechnology and MedicalEngineering NationalInstitute of Technology Rourkela Rourkela 769008 India Fax 91 661 2462999 Tel 91 661 2462284 E-mail subhankar_paul@ spaul@ T. K. Chaudhuri Department of Biochemical Engineering and Biotechnology Indian Institute of Technology Delhi Hauz Khas New Delhi 110016 India Fax 91 11 2658 2282 Tel 91 11 2659 1012 E-mail tapan@ Received 4 August 2007 revised 27 September 2007 accepted 1 October 2007 doi In vitro refolding of maltodextrin glucosidase a 69 kDa monomeric Escherichia coli protein was studied in the presence of glycerol dimethylsulfoxide trimethylamine-N-oxide ethylene glycol trehalose proline and chaperonins GroEL and GroES. Different osmolytes namely proline glycerol trimethylamine-N-oxide and dimethylsulfoxide also known as chemical chaperones assist in protein folding through effective inhibition of the aggregation process. In the present study it was observed that a few chemical chaperones effectively reduced the aggregation process of maltodextrin glucosidase and hence the in vitro refolding was substantially enhanced with ethylene glycol being the exception. Although the highest recovery of active maltodextrin glucosidase was achieved through the ATP-mediated GroEL GroES-assisted refolding of denatured protein the yield of correctly folded protein from glycerol- or proline-assisted spontaneous refolding process was closer to the chaperonin-assisted refolding. It was also observed

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