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A cell surface displayed system in  Pichia pastoris  GS115 was developed by using GCW61, a glycosylphosphatidylinositol-modified cell wall protein from  P. pastoris , as the anchor protein.  Thermomyces lanuginosus  lipase ( TL L) was successfully displayed on the  P. pastoris  cell wall by fusing GCW61 gene with  TL L2 gene (NCBI Accession:  O59952 ) that was optimized with codon bias and synthesized. Cell surface displayed  TL L2 was confirmed by the immunofluorescence microscopy. Flask fermentation was performed for 144 h with lipase activity up to 1964.76 U/g. Enzymatic properties of cell surface displayed  TL L2 were also investigated. Displayed  TL L2 occurred the maximum activity at pH 9 and 55°C and demonstrated characteristics of wide thermal adaptability and alkaline pH resistance. The optimum substrate was  p -nitrophenyl hexanoate. Bivalent metal ions Ca 2+ , Mn 2+ , and Zn 2+  had the activation effect on displayed  TL L2, while Cu 2+ , Fe 2+ , Fe 3+ , K + , Li + , Na + , and Co 2+  ions had the inhibitory effect on it. Since cell surface displayed  TL L2 required less purification steps compared with free enzyme and showed high enzyme activities, it would be able to be further applied in various potential applications.

Cell Surface Display of Thermomyces lanuginosus Lipase in Pichia pastoris