scispace - formally typeset
Search or ask a question

What are the reasons behind protein loss expressed in E.coli during fermentation process? 


Best insight from top research papers

Protein loss in E. coli during fermentation can be attributed to various factors. Firstly, the drop in viable cell count post-induction may reflect a loss of cell division capability rather than cell death, impacting protein production. Additionally, the appearance of plasmid-losing cells during cell fission can lead to protein loss, emphasizing the need for strategies to maintain plasmid stability. Moreover, overproduction of NADPH in the pentose phosphate pathway can repress cell growth, affecting protein expression levels. Furthermore, high-level over-expression of both soluble and integral membrane proteins can result in significant cell loss, impacting protein yields. Understanding these factors is crucial for optimizing recombinant protein expression in E. coli fermentation processes.

Answers from top 5 papers

More filters
Papers (5)Insight
High-level over-expression of both soluble and integral membrane proteins in E. coli triggers >99.9% cell loss, leading to an adaptive survival response akin to antimicrobial resistance development.
Protein loss in E. coli during fermentation is due to variations in gene expression, such as ptsG degradation, affecting glucose consumption and biomass concentration, as observed in pgi mutants.
Protein loss in E. coli during fermentation is due to plasmid instability caused by cell fission generating plasmid-losing cells, leading to competitive advantage and rapid population dominance.
Metabolic burden, inclusion bodies, and inefficient translocation contribute to protein loss during E. coli fermentation, emphasizing the need for optimizing transcription to enhance recombinant protein production efficiency.
Protein loss in E. coli during fermentation is mainly due to a drop in cell division capability, not cell death, as observed in recombinant protein production processes.

Related Questions

Why after fermentation, protein is aggregation?5 answersProtein aggregation after fermentation can occur due to various factors. During industrial production, proteins like monoclonal antibodies may aggregate at different stages, compromising their quality and efficacy. Proteins tend to aggregate, especially when stored at high concentrations, impacting stability and therapeutic properties. In the case of Lactobacillus brevis, aggregation is triggered by glucose fermentation, causing surface layer protein detachment and subsequent aggregation. Protein function relies on a defined 3D structure, with unfolding and aggregation affecting functionality. Recombinant proteins in genetically engineered organisms often form inclusion bodies due to aggregation, although recent studies suggest potential applications in various biotechnological fields. Overall, protein aggregation post-fermentation is a critical concern affecting protein stability, bioavailability, and therapeutic effectiveness.
How does the fermentation process affect the formation and stability of emulsions?4 answersThe fermentation process plays a crucial role in enhancing the formation and stability of emulsions. Fermentation with lactic acid bacteria can lead to the modification of food ingredients, such as phosvitin, into peptides that improve emulsifying properties and bioactivity. Microorganisms used in fermentation can create emulsifiers capable of forming reverse micelles, aiding in the effective penetration and absorption of bioactive substances into the skin, thus improving emulsion stability and skin cell toxicity. Additionally, the stability of emulsions can be attributed to factors like stirring velocity, time, and the ratios of surfactants to oil, which influence droplet size, phase viscosity, and coalescence, preventing settling or separation during fermentation. Yeast cells, depending on their physiological state and cultivation medium, can also contribute to the stability of emulsions through mechanisms like electrostatic repulsion between droplets.
What happens during fermentation?5 answersDuring fermentation, carbohydrates are converted into alcohol or organic acids by microorganisms like yeasts or bacteria under anaerobic conditions. This process has been utilized for thousands of years to produce various products, including alcoholic beverages like wine and beer. Fermentation can lead to the production of low molecular-weight peptides from proteins in both animal-based and plant-based foods, offering health benefits such as antimicrobial, antioxidant, and antidiabetic properties. Additionally, fermentation is a biochemical change induced by microorganisms that can transform perishable raw materials into safe, shelf-stable foods through the production of acids or alcohols. The process involves controlling variables like strain, temperature, and viscosity to ensure successful fermentation and product quality.
How do fermentation processes affect the stable isotope composition of food?5 answersFermentation processes do not substantially affect the stable isotope composition of grain-based foods. The isotopic signatures of multi-ingredient foods can be accurately estimated using mass-balance equations based on the isotopic composition of their constituent raw ingredients. The isotopic parameters of fermentation products can be used to characterize their carbohydrate precursors, and variations in reaction rates induced by the fermentation medium do not introduce isotopic fractionation effects. The composition of the fermentation medium does not significantly influence the isotopic ratios of the fermentation products, supporting the use of isotopic analysis to characterize sugars in different fruit juices. The fermentation of food using carboxylic acid fermentation has been found to reduce the risk of contamination by infective microorganisms. The present invention suggests using fatty acid oxidizing enzymes in fermentation processes, including for ethanol production, along with additional enzymes and growth stimulators for the fermenting microorganisms.
Why do some Escherichia albertii strains ferment lactose while others do not?5 answersEscherichia albertii strains can either ferment lactose or not due to genetic differences. Some strains of E. albertii have been found to be lactose-negative, meaning they are unable to ferment lactose. This inability to ferment lactose is a distinguishing characteristic of E. albertii and can be used to differentiate it from other Enterobacteriaceae. On the other hand, other strains of E. albertii have been found to be lactose-positive, meaning they are able to ferment lactose. The ability to ferment lactose is determined by the presence or absence of specific genes in the E. albertii strains. Further research is needed to understand the genetic basis for lactose fermentation in E. albertii and the implications it may have on the pathogenicity and virulence of different strains.
What fermentation conditions in prokaryotic expression affect protein homogeneity?5 answersFermentation conditions in prokaryotic expression can affect protein homogeneity. The culture conditions, such as pH, temperature, shaking speed, and oxygen supply, play a significant role in protein expression at large scale. High cell density anaerobic fermentation can result in a fermentation broth with a high protein yield. Redox potential-driven fermentation can guide the cultivation progress of recombinant protein expression and improve protein activity. Heterogeneous activation of the secretion stress pathway can lead to expression heterogeneity of secretory proteins in Bacillus subtilis, but this can be suppressed by degU mutation and optimized growth conditions. The invention of a high-density fermenting method and an improved culture medium can improve protein homogeneity in prokaryotic expression.

See what other people are reading

What does moisture content in propolis affect?
5 answers
The moisture content in propolis affects various aspects such as the physicochemical properties, antioxidant capacity, and stability of bioactive compounds. High moisture content can impact the flow properties of propolis powders and alter the crystalline structure when encapsulated. Propolis with moisture content ranging from 1.96% to 8.26% showed variability in physicochemical parameters and antioxidant activity, indicating the importance of moisture levels in determining propolis quality. Additionally, moisture content in raw propolis samples collected from different regions ranged from 0.98% to 2.97%, influencing the total phenolics and flavonoids content, which are crucial for the antioxidant potential of propolis. Therefore, controlling and maintaining optimal moisture content in propolis is essential for preserving its bioactive compounds and ensuring its beneficial properties.
What is the role of lipids in maintaining cell membrane function and structure?
5 answers
Lipids play crucial roles in maintaining cell membrane function and structure. They are not just structural components but also act as molecular chaperones, topological determinants, and organizers of biological machines. Lipids are essential for stabilizing membrane protein structures, mediating protein-protein interactions, and maintaining specific conformational states of membrane proteins. Furthermore, alterations in membrane lipid metabolism are associated with major diseases, highlighting the importance of understanding lipid diversity and their roles in cell signaling. Lipids also contribute to the mechanical stability of cell membranes, modulating their physical properties and affecting bilayer thickness and lipid ordering. Overall, lipids are dynamic molecules that interact with proteins, regulate cellular functions, and are vital for the integrity and functionality of cell membranes.
How does the RAS gene contribute to the development of preeclampsia?
5 answers
The renin-angiotensin system (RAS) plays a crucial role in the pathogenesis of preeclampsia (PE). Dysregulation of the RAS gene components, such as angiotensin-converting enzyme (ACE) and angiotensin II (Ang II), contributes to the development of PE. Genetic variations in the ACE gene, like the rs4343 polymorphism, have been associated with an increased risk of PE. Additionally, the overactivation of the Ang II/ACE/AT1R axis, along with decreased levels of protective components like ACE 2/Ang 1–7/MasR, can lead to hypertension characteristic of PE. Furthermore, studies suggest that the compensatory alterations in the RAAS during normal pregnancy are disrupted in PE, leading to a disturbance in the delicate equilibrium necessary for maternal and fetal well-being. These findings highlight the intricate involvement of the RAS gene in the pathogenesis of preeclampsia.
What distubs the cycle of hormones?
5 answers
Disturbances in the cycle of hormones can be influenced by various factors such as adiposity, hormonal administration methods, and interactions between steroid hormones and growth factors. Adiposity, particularly central adiposity, has been linked to alterations in sex hormone patterns across the menstrual cycle, affecting levels of estradiol, progesterone, luteinizing hormone, and follicle-stimulating hormone. Additionally, methods of hormonal administration for contraception and menstrual cycle regulation, involving progestins and estrogen-progestin combinations, can impact the hormonal balance. Furthermore, the interplay between steroid hormones and growth factors can affect cell cycle regulation, proliferation, and differentiation, highlighting the importance of understanding these interactions in maintaining hormonal homeostasis. These factors collectively contribute to disturbances in the hormonal cycle, emphasizing the complexity of hormonal regulation in the body.
Do PD-L1 inhibitors slow TNBC xenograft growth in nude mice?
5 answers
PD-L1 inhibitors have shown efficacy in slowing TNBC xenograft growth in nude mice. Studies using a murine breast cancer model demonstrated that anti-PD-L1 treatment significantly suppressed primary tumor growth and extended survival. Additionally, in a study involving a syngeneic mouse tumor model, Dato-DXd, an ADC targeting TROP2, enhanced antitumor activity when combined with PD-1/PD-L1 inhibitors, suggesting a potential synergy in inhibiting tumor growth. Furthermore, PD-1 blockade in nude mice resulted in decreased tumor growth, indicating the importance of PD-1 signaling in promoting tumor progression. These findings collectively support the notion that PD-L1 inhibitors can effectively slow TNBC xenograft growth in nude mice, highlighting their potential as a therapeutic strategy for TNBC.
What is the concentration of calcein AM and propidium iodide for cell viability?
5 answers
The concentration of calcein-AM used for cell viability assessments varies depending on the study. In one research, calcein-AM was employed as a sensitive tool for detecting intracellular ROS generation in living cells, with a higher sensitivity compared to other fluorescein derivatives. On the other hand, propidium iodide (PI) was utilized in dynamic cell viability assays at concentrations of 1.5 or 7.5 microM, showing minimal effects on cell cycle progression and DNA replication in human cells. Additionally, a double-staining procedure using fluorescein diacetate and propidium iodide was established for cell viability determination in cell suspension, providing a simple and viable method for quantitative and qualitative analysis. Therefore, the concentration of calcein-AM and propidium iodide for cell viability assessments can range from sensitive ROS detection to minimal impact on cell cycle progression, depending on the specific experimental requirements.
What is the name of the gene for perchloric acid-soluble protein?
5 answers
The gene for perchloric acid-soluble protein is named differently in various organisms. In Trichomonas vaginalis, the gene for this protein is identified as tv-psp1. In rats, the gene for this protein is referred to as L-PSP. Moreover, in the rat lung, the gene for perchloric acid-soluble protein is designated as RLu-PSP1. These proteins play crucial roles in inhibiting protein synthesis, regulating cell proliferation, and responding to cellular stressors, showcasing their significance in various biological processes across different species.
What is the role of metabolism in the development and progression of cancer cells?
5 answers
Metabolism plays a crucial role in the development and progression of cancer cells by supporting their growth, proliferation, and survival. Cancer cells exhibit unique metabolic profiles, characterized by increased reliance on glucose, glutamine, and other nutrients to generate energy and macromolecules needed for rapid division. Oncogenic signaling triggers metabolic reprogramming, directing cancer cells to prioritize anabolic processes for biosynthesis over energy production, promoting cell growth and resistance to cell death. Alterations in lipid metabolism also contribute significantly to cancer biology, impacting various stages of the disease, including metastasis and therapeutic resistance. Understanding these metabolic changes and their interplay with signaling pathways is crucial for identifying potential therapeutic targets to combat cancer progression and drug resistance.
What is the role of the Pentose Phosphate Pathway in cancer pathogenesis?
5 answers
The Pentose Phosphate Pathway (PPP) plays a crucial role in cancer pathogenesis by providing NADPH, nucleotides, and metabolic intermediates essential for cancer cell proliferation, redox balance, and survival. Cancer cells often exhibit upregulated PPP activity to support rapid growth, DNA synthesis, and antioxidant responses. Specifically, enzymes like glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) within the PPP are frequently overexpressed in cancer, influencing DNA repair, redox homeostasis, and cell cycle regulation. The PPP also contributes to maintaining energy levels, promoting survival, and inducing cellular proliferation in cancer cells through various metabolic pathways. Overall, the PPP emerges as a critical regulator of cancer cell metabolism, highlighting its significance in cancer pathogenesis.
What genes need to be overexpressed, downexpressed or deleted to improve lysine production in Escherichia Coli?
5 answers
To enhance lysine production in Escherichia coli, various genetic modifications can be implemented. Overexpressing lysine biosynthesis enzymes like lysine-α-ketoglutarate reductase and saccharopine dehydrogenase, as well as α-aminoadipate-δ-semialdehyde dehydrogenase, can boost lysine production. Additionally, optimizing the expression of top-demanded proteins and regulating energy metabolism-related proteins can significantly increase lysine titers. Furthermore, modifying E. coli coding and noncoding regions can lead to enhanced lysine production for various applications. Moreover, utilizing the MAGE technique for gene alterations, such as upregulation and downregulation/deletion of specific genes, can optimize the fermentation process for L-lysine production on an industrial scale. These genetic manipulations collectively contribute to improving lysine production in E. coli.
How is BCL2 involved in chemoresistance in OSCC?
5 answers
Bcl-2 plays a crucial role in chemoresistance in Oral Squamous Cell Carcinoma (OSCC). Studies have shown that Bcl-2 is upregulated in OSCC cells, leading to resistance against chemotherapeutic agents like cisplatin. This overexpression of Bcl-2 contributes to cancer development and resistance to current anticancer treatments in OSCC. Inhibition of Bcl-2 using specific inhibitors like ABT-199 has been found to effectively target OSCC cells by inhibiting proliferation and inducing apoptosis, thereby sensitizing them to chemotherapy. Additionally, targeting Bcl-2 has been shown to augment the effects of cisplatin in eliminating OSCC cells both in vitro and in vivo. Therefore, Bcl-2 inhibition presents a promising strategy to overcome chemoresistance in OSCC and enhance the efficacy of existing treatments.