ArticleMicrobial cell factories2011
Modeling and measuring intracellular fluxes of secreted recombinant protein in Pichia pastoris with a novel 34S labeling procedure.
Article in Microbial cell factories, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 41 citations in OpenAlex.
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- Engineering of the unfolded protein response pathway in Pichia pastoris: enhancing production of secreted recombinant proteins.Applied microbiology and biotechnology · 2021Review
- Secretion of a low and high molecular weight β-glycosidase by Yarrowia lipolytica.Microbial cell factories · 2020Article
- Comprehensive comparison of Yarrowia lipolytica and Pichia pastoris for production of Candida antarctica lipase B.Scientific reports · 2020Article
- Single-Cell Approach to Monitor the Unfolded Protein Response During Biotechnological Processes WithFrontiers in microbiology · 2019Article
- Application of Continuous Culture Methods to Recombinant Protein Production in Microorganisms.Microorganisms · 2018Review
- Investigating the effect of carbon source on rabies virus glycoprotein production in Pichia pastoris by a transcriptomic approach.MicrobiologyOpen · 2017Article
- Effects of UPR and ERAD pathway on the prolyl endopeptidase production in Pichia pastoris by controlling of nitrogen source.Journal of industrial microbiology & biotechnology · 2017Article
- The effect of hypoxia on the lipidome of recombinant Pichia pastoris.Microbial cell factories · 2017Article
- Engineering the supply chain for protein production/secretion in yeasts and mammalian cells.Journal of industrial microbiology & biotechnology · 2015Review
- Overall Key Performance Indicator to Optimizing Operation of High-Pressure Homogenizers for a Reliable Quantification of Intracellular Components in Pichia pastoris.Frontiers in bioengineering and biotechnology · 2015Article
- Model based engineering of Pichia pastoris central metabolism enhances recombinant protein production.Metabolic engineering · 2014Article
- Article
- In Pichia pastoris, growth rate regulates protein synthesis and secretion, mating and stress response.Biotechnology journal · 2014Article
- Sulfur-34S stable isotope labeling of amino acids for quantification (SULAQ34) of proteomic changes in Pseudomonas fluorescens during naphthalene degradation.Molecular & cellular proteomics : MCP · 2013Article
- Quantitative metabolomics analysis of amino acid metabolism in recombinant Pichia pastoris under different oxygen availability conditions.Microbial cell factories · 2012Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe budding yeast Pichia pastoris is widely used for protein production. To determine the best suitable strategy for strain improvement, especially for high secretion, quantitative data of intracellular fluxes of recombinant protein are very important. Especially the balance between intracellular protein formation, degradation and secretion defines the major bottleneck of the production system. Because these parameters are different for unlimited growth (shake flask) and carbon-limited growth (bioreactor) conditions, they should be determined under "production like" conditions. Thus labeling procedures must be compatible with minimal production media and the usage of bioreactors. The inorganic and non-radioactive 34S labeled sodium sulfate meets both demands.
resultsWe used a novel labeling method with the stable sulfur isotope 34S, administered as sodium sulfate, which is performed during chemostat culivations. The intra- and extracellular sulfur 32 to 34 ratios of purified recombinant protein, the antibody fragment Fab3H6, are measured by HPLC-ICP-MS. The kinetic model described here is necessary to calculate the kinetic parameters from sulfur ratios of consecutive samples as well as for sensitivity analysis. From the total amount of protein produced intracellularly (143.1 μg g-1 h-1 protein per yeast dry mass and time) about 58% are degraded within the cell, 35% are secreted to the exterior and 7% are inherited to the daughter cells.
conclusionsA novel 34S labeling procedure that enables in vivo quantification of intracellular fluxes of recombinant protein under "production like" conditions is described. Subsequent sensitivity analysis of the fluxes by using MATLAB, indicate the most promising approaches for strain improvement towards increased secretion.
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