ArticlePloS one2013
de novo design and synthesis of Candida antarctica lipase B gene and α-factor leads to high-level expression in Pichia pastoris.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Yarrowia lipolytica and Komagataella phaffii (Pichia pastoris) as Hosts for Heterologous Expression of Lipases.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Strains and Molecular Tools for Recombinant Protein Production in Pichia pastoris.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Efficient expression vectors and host strain for the production of recombinant proteins by Yarrowia lipolytica in process conditions.Microbial cell factories · 2019Article
- Streamlined Preparation of ImmobilizedACS omega · 2017Article
- Recent advances of molecular toolbox construction expand Pichia pastoris in synthetic biology applications.World journal of microbiology & biotechnology · 2017Review
- Engineering Translation in Mammalian Cell Factories to Increase Protein Yield: The Unexpected Use of Long Non-Coding SINEUP RNAs.Computational and structural biotechnology journal · 2016Review
- Gene and protein sequence optimization for high-level production of fully active and aglycosylated lysostaphin in Pichia pastoris.Applied and environmental microbiology · 2014Article
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4 authors at 2 institutions in 1 country.
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Abstract
Candida antarctica lipase B (CALB) is one of the most widely used and studied enzymes in the world. In order to achieve the high-level expression of CALB in Pichia, we optimized the codons of CALB gene and α-factor by using a de novo design and synthesis strategy. Through comparative analysis of a series of recombinants with different expression components, we found that the methanol-inducible expression recombinant carrying the codon-optimized α-factor and mature CALB gene (pPIC9KαM-CalBM) has the highest lipase production capacity. After fermentation parameters optimization, the lipase activity and protein content of the recombinant pPIC9KαM-CalBM reached 6,100 U/mL and 3.0 g/L, respectively, in a 5-L fermentor. We believe this strategy could be of special interest due to its capacity to improve the expression level of target gene, and the Pichia transformants carrying the codon-optimized gene had great potential for the industrial-scale production of CALB lipase.
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