Abstract
The influence of number of signal peptide cleavage site on extracellular production of recombinant cutinase was described in the present work. Firstly, recombinant Escherichia coli BL/pET-CUT1 and BL/pET-CUT2 that expressed precursor cutinase with one and two signal peptide cleavage sites were constructed, respectively. Under the different culture condition, cutinase activity in periplasm and medium of BL/pET-CUT2 were higher than that of BL/pET-CUT1. When cultured in 30°C with glycerol of 10g/l, 85.2U/ml cutinase activity was detected in periplasm of BL/pET-CUT2 after 40h cultivation, while 44.6U/ml was found in BL/pET-CUT1. It also was found that the cutinase activity in culture medium of BL/pET-CUT 2 reached to 130.3U/ml while the activity of BL/pET-CUT 1 reached to 95.7U/ml after 64h of culture. From this investigation we have found that the increase of signal peptide cleavage site can improve the extracellular production of recombinant cutinase in E. coli.
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