ArticleJournal of industrial microbiology & biotechnology2013
Efficient secretion of lipase r27RCL in Pichia pastoris by enhancing the disulfide bond formation pathway in the endoplasmic reticulum.
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Biosynthesis and metabolic engineering of natural sweeteners.AMB Express · 2025Review
- Understanding exopolysaccharide byproduct formation in Komagataella phaffii fermentation processes for recombinant protein production.Microbial cell factories · 2024Article
- Article
- Engineering of the unfolded protein response pathway in Pichia pastoris: enhancing production of secreted recombinant proteins.Applied microbiology and biotechnology · 2021Review
- Synergistic optimisation of expression, folding, and secretion improves E. coli AppA phytase production in Pichia pastoris.Microbial cell factories · 2021Article
- Production and secretion dynamics of prokaryotic Penicillin G acylase in Pichia pastoris.Applied microbiology and biotechnology · 2020Article
- Improving the Thermostability ofFrontiers in microbiology · 2020Article
- Different construction strategies affected on the physiology of Pichia pastoris strains highly expressed lipase by transcriptional analysis of key genes.Bioengineered · 2019Article
- Identification of novel factors enhancing recombinant protein production in multi-copy Komagataella phaffii based on transcriptomic analysis of overexpression effects.Scientific reports · 2017Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lipase r27RCL from Rhizopus chinensis CCTCC M201021 was heterologously expressed in Pichia pastoris GS115 by simultaneous co-expression with two secretion factors ERO1p and PDI involved in the endoplasmic reticulum (ER). Compared to the expression of the lipase alone (12,500 U/ml), co-expression with these two proteins resulted in the production of larger total quantities of enzymes. The largest increase was seen when the combined ERO1p/PDI system was co-expressed, resulting in approximately 30 % higher enzyme yields (16,200 U/ml) than in the absence of co-expressed secretion factors. The extracellular protein concentration of the recombinant strain Co XY RCL-5 reached 9.39 g/l in the 7-l fermentor. Simultaneously, the fermentation time was also shortened by about 8 h compared to that of the control. The substrate-specific consumption rate (Qs) and the product-specific production rate (Qp) were both investigated in this research. In conclusion, the space-time yield was improved by co-expression with ERO1p and PDI. This is a potential strategy for high level expression of other heterologous proteins in P. pastoris.
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