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Background  For industrial bioconversion processes, the utilization of surface-displayed lipase in the form of whole-cell biocatalysts is more advantageous, because the enzymes are displayed on the cell surface spontaneously, regarded as immobilized enzymes.    Results  Two  Pichia pastoris  cell surface display vectors based on the flocculation functional domain of FLO with its own secretion signal sequence or the α-factor secretion signal sequence were constructed respectively. The lipase gene  lipB52  fused with the  FLO  gene was successfully transformed into  Pichia pastoris  KM71. The lipase LipB52 was expressed under the control of the  AOX1  promoter and displayed on  Pichia pastoris  KM71 cell surface with the two  Pichia pastoris  cell surface display vectors. Localization of the displayed LipB52 on the cell surface was confirmed by the confocal laser scanning microscopy (CLSM). The LipB52 displayed on the  Pichia pastoris  cell surface exhibited activity toward  p -nitrophenol ester with carbon chain length ranging from C 10  to C 18 , and the optimum substrate was  p -nitrophenol-caprate (C 10 ), which was consistent with it displayed on the  Saccharomyces cerevisiae  EBY100 cell surface. The hydrolysis activity of lipase LipB52 displayed on  Pichia pastoris  KM71-pLHJ047 and KM71-pLHJ048 cell surface reached 94 and 91 U/g dry cell, respectively. The optimum temperature of the displayed lipases was 40°C at pH8.0, they retained over 90% activity after incubation at 60°C for 2 hours at pH 7.0, and still retained 85% activity after incubation for 3 hours.    Conclusion  The LipB52 displayed on the  Pichia pastoris  cell surface exhibited better stability than the lipase LipB52 displayed on  Saccharomyces cerevisiae  cell surface. The displayed lipases exhibited similar transesterification activity. But the  Pichia pastoris  dry cell weight per liter (DCW/L) ferment culture was about 5 times than  Saccharomyces cerevisiae , the lipase displayed on  Pichia pastoris  are more suitable for whole-cell biocatalysts than that displayed on  Saccharomyces cerevisiae  cell surface.

bmc biotechnology

Efficient display of active lipase LipB52 with a Pichia pastoris cell surface display system and comparison with the LipB52 displayed on Saccharomyces cerevisiae cell surface