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- W2890113626 abstract "The protein Loosenin 1 from the wood degrading fungus Bjerkandera adu-sta (BaLOOS1) has been shown to loosen up recalcitrant biomass and en-hance enzymatic saccharification. BaLOOS1 is the only loosenin protein that has been biochemically characterised so far. An earlier attempt to ex-press BaLOOS1 in Pichia pastoris, with its native signal peptide (SP), indi-cated low expression level (T. Haataja and J. Stahlberg, unpublished).The purpose of this study was to exchange the native SP of BaLOOS1 in an attempt to obtain higher expression levels. A pGAP P. pastoris expression plasmid was used that contained the gene for BaLOOS1 with an appended C-terminal His tag, and the native SP was exchanged by Gibson assembly followed by transformation into P. pastoris X33-strain. Four SPs were tested. Two SPs were from loosenin homologs in Trichoderma reesei and P. pastoris, respectively, from a previous study. The two other SPs were the α-factor from Saccharomyces cerevisiae and the Epx1-SP from the most abun-dant secretory protein Epx1 in P. pastoris. All the SP constructs were suc-cessfully inserted. The T. reesei SP gave the strongest band of the expected molecular weight on SDS-PAGE gel of the tested SPs indicating a higher expression level than the others. Specific binding to an IMAC column strongly suggests that the expressed protein is the His-tagged BaLOOS1. However, definite confirmation of the identity remains to be done, e.g. by peptide mapping." @default.
- W2890113626 created "2018-09-27" @default.
- W2890113626 creator A5010536492 @default.
- W2890113626 date "2018-08-17" @default.
- W2890113626 modified "2023-09-26" @default.
- W2890113626 title "Signal peptide exchange for higher expression of Bjerkandera adusta Loosenin 1 in P. pastoris" @default.
- W2890113626 hasPublicationYear "2018" @default.
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