Extracellular expression of YlLip11 with a native signal peptide from Yarrowia lipolytica MSR80 in three different yeast hosts

Protein Expression and Purification
Arti KumariRani Gupta

Abstract

Lipase YlLip11 from Yarrowia lipolytica was expressed with a signal peptide encoding sequence in Arxula adeninivorans, Saccharomyces cerevisiae and Hansenula polymorpha using the Xplor®2 transformation/expression platform and an expression module with the constitutive Arxula-derived TEF1 promoter. The YlLip11 signal peptide was functional in all of the yeast hosts with 97% of the recombinant enzyme being secreted into the culture medium. However, recombinant YlLip11 with His Tag fused at C-terminal was not active. The best recombinant YlLip11 producing A. adeninivorans G1212/YRC102-YlLip11 transformant cultivated in shake flasks produced 2654 U/L lipase, followed by S. cerevisiae SEY6210/YRC103-YlLip11 (1632U/L) and H. polymorpha RB11/YRC103-YlLip11 (1144U/L). Although the biochemical parameters of YlLip11 synthesized in different hosts were similar, their glycosylation level and thermo stability differed. The protein synthesized by the H. polymorpha transformant had the highest degree of glycosylation and with a t1/2 of 60min at 70°C, exhibited the highest thermostability.

References

Jun 4, 2004·Journal of Industrial Microbiology & Biotechnology·Yaroslav TerentievGotthard Kunze
Oct 10, 2007·Applied Microbiology and Biotechnology·Erik BöerGerd Gellissen
Apr 21, 2011·Journal of Agricultural and Food Chemistry·Kuo-Sheng HungShye-Jye Tang
Jan 17, 2012·Applied Biochemistry and Biotechnology·Xiaofeng WangYunjun Yan

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Citations

May 24, 2019·Frontiers in Bioengineering and Biotechnology·João Heitor Colombelli Manfrão-NettoNádia Skorupa Parachin
Jun 11, 2021·Applied Microbiology and Biotechnology·Daniel Ruben Akiola SanyaMahesh B Khot

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