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A novel Lip +Pichia pastoris  expression platform was developed by integrating lipase Lip2 from  Yarrowia lipolytica  under constitutive Glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. Effective expression of reporter protein amylase from  Bacillus licheniformis  was achieved utilizing methyloleate in Lip + Amy + host. Lipase hydrolyzed methyloleate into methanol that sustained PAOX1induction, and oleic acid, which was readily utilized as a carbon source. The protein expression achieved in presence of methyloleate was comparable to methanol-induced cells, along with an increase in productive biomass. In Lip + Amy +  host, total amylase production of 220.9 ± 13 U/mg biomass was achieved at 96 h using methyloleate supplemented every 24 h. While 206.0 ± 17 U/mg biomass was obtained at 108 h in an Amy +  host induced with methanol every 12 h. Further, lipase expression neither affected growth nor added additional burden on the cellular machinery and no oleic acid accumulation was observed at any time point due to its emulsification and efficient utilization by lipase positive host. Similar results obtained with the second reporter protein  γ- cyclodextrin glycosyltransferase (CGTase) from  Evansella caseinilytica  validated the platform. An alternate lipase Lip11 from  Y .  lipolytica  was also employed in developing a Lip +  host to validate disparity between lipase background and PAOX1induction in presence of methyloleate.

preparative biochemistry and biotechnology

Development of a novel  Pichia pastoris  expression platform  via  genomic integration of lipase gene for sustained release of methanol from methyloleate