"Freezing" application in 3 biopharmaceuticals systems: Cryoprotection of protein

Cryoprotection of protein

As a unique biopolymer, protein can be used as a delivery vector for therapeutic substances. Protein has important characteristics, such as bioavailability, biocompatibility and biodegradability, and low toxicity. It can be used as a delivery platform for various small molecule therapies, gene therapy, protein biologics, and cells. While freezing is widely used in the manufacturing process of protein therapeutics, cryoprotection may lead to loss of biological activity. The following are the relevant precautions for your integrated protein cryoprotection:

Further Reading: The application of protein (Already in the works...)

  • Protein is usually stored in frozen conditions or a lyophilized state, which is usually better than liquid storage because the solid state will increase stability and shelf life.
  • When quenching freezing, the addition of surfactants always leads to an improvement in the recovery of LDH activity. The addition of 0.01% w/v Tween 80 significantly reduces protein aggregation and usually leads to an increase in protein activity.
  • In the thawing, the addition of Tween 80 leads to a decrease in the recovery of protein activity. The possible explanation is that the surfactant has an effect on the conformation of the protein at low pH.
  • In quenched samples containing cryoprotectants and without surfactants, all protein recovery rates show an increase compared with the formulations using buffer only.
  • The addition of excipients improves the recovery of protein activity after freezing and thawing. This effect is particularly obvious in the presence of Tween 80.
  • Fast thawing may be beneficial for both bulk denaturation and surface denaturation of proteins because it minimizes the process duration and the risk of recrystallization.
  • If the stability of the frozen protein in the solution is poor, a high cooling rate should be the first choice, so that the protein is quickly immobilized in the glass matrix.
  • If the protein is more stable in the bulk solution than at the ice interface, the freezing process should be designed to produce a small ice-water surface area.

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