Cell Cultured Milk Proteins

We use fermentation based techniques derived from biotechnology to recreate the essential protein ingredients that are found in colostrum milk. As a start, we take bacteria that carry the genes coding for milk components and use them as factories that produce milk components for us. we later employ various purification techniques to isolate the milk proteins from the bacteria  and finally arrive with a chemically pure functional milk component product

Composition of Human Colostrum

Human breast milk (HBM) is essential for the infant’s growth and development right after birth and is an irreplaceable source of nutrition for early human survival. Various infant formulas have many similarities to HBM in many components, but there is no perfect substitute for HBM.

Human colostrum, the first milk produced after birth, has a unique composition that differs from mature breast milk. Colostrum is low in fat but high in protein and relatively rich in immune-protective components and Growth Factors. Here are the key components of human colostrum:

Immune Factors

Rich in immunologic components like secretory IgA, lactoferrin, and leukocytes

Growth Factors

Contains higher concentrations of growth factors, including epidermal growth factor

Antimicrobial Peptides

High levels of antimicrobial peptides like lactoferrin, Lysozyme and lactoperoxidase

Growth factors play an important roles in infant development, particularly in gastrointestinal maturation, immune system development, and overall growth regulation.

The concentrations of these growth factors tend to be highest in colostrum and early milk, gradually decreasing over the course of lactation. However, they remain present throughout at least the first 6 months of breastfeeding.

The composition and concentrations of growth factors can vary based on factors like gestational age of the infant, with milk from mothers of extremely preterm infants often containing higher levels of certain growth factors like EGF and TGF-α.

Human breast milk contains several important growth factors, including:

  1. Epidermal Growth Factor (EGF):
    • Present in high concentrations, especially in early milk/colostrum
    • Levels are highest in the first days after birth and gradually decrease over the first 2 weeks of lactation
    • Concentrations are significantly higher in milk from mothers of extremely preterm infants compared to full-term infants
  1. Vascular Endothelial Growth Factor (VEGF):
    • Present in very high concentrations in early breast milk
  1. Hepatocyte Growth Factor (HGF):
    • Present in very high concentrations in early breast milk
  1. Transforming Growth Factor-α (TGF-α):
  1. Insulin-like Growth Factors (IGF-1 and IGF-2)
    • Heparin-Binding EGF-like Growth Factor (HB-EGF)
    • Granulocyte Colony Stimulating Factor (G-CSF

 

 

Recombinant protein production in Escherichia coli (E. coli) involves several steps and poses various challenges. E. coli is commonly used for this purpose due to its well-established status as a cell factory for protein production, which lowers the costs and improves the yield of recombinant proteins. However, there are several challenges associated with this process, including the potential for protein toxicity to the host, aggregation in inclusion bodies, and the lack of post-translational modifications in prokaryotic cells, which can lead to protein misfolding and aggregation.To address these challenges, various strategies have been developed, such as optimizing protein expression, enhancing solubility, improving correct folding efficiency, and alleviating the host burden associated with protein overproduction. Despite these challenges, with careful selection of host strains, vectors, and growth conditions, most recombinant proteins can be cloned and expressed at high levels in E. coli

Eukaryotic expression systems offer a range of options for the production of recombinant proteins, each with its own advantages and considerations. The most commonly used expression systems are based on:

  1. Stably Transfected Adherent CHO Cells or Nonadherent Lymphoid Cell Lines: These systems are often used for the production of recombinant proteins, including therapeutics and research tools.
  2. Infection of Insect Cells by Recombinant Baculoviruses: This is an efficient alternative for the expression of recombinant proteins.
  3. Transient Expression in Mammalian Cells (e.g., COS Cells): This is often used for the production of smaller quantities of proteins.

The choice of a suitable expression system depends largely on the biochemical and biological properties of the protein of interest, as well as the nature of the planned experiments and the amount of recombinant protein required.

These systems offer the advantage of post-translational modifications, which are important for the proper folding and function of many proteins. The selection of the most suitable system is crucial for the successful production of recombinant proteins based on the specific requirements of the protein and the intended application

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