A method for purifying a bioengineered elastin-like protein
CN119613535BActive Publication Date: 2026-06-19XIANGFU LAB +1
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- XIANGFU LAB
- Filing Date
- 2025-01-09
- Publication Date
- 2026-06-19
AI Technical Summary
Technical Problem
Existing technologies rely too heavily on efficient purification methods for K proteins using His-tagged peptides, making it difficult for protein products to be approved for use in biopharmaceuticals.
Method used
A bioengineering-based purification method was adopted, including steps such as bacterial resuspension, thermal lysis, rapid cooling, cation exchange chromatography, and ultrafiltration desalting. The heat resistance and charge properties of K protein were utilized for purification, reducing dependence on His-tagged peptides.
Benefits of technology
It improves protein purity and yield, reduces purification costs, simplifies purification steps, is suitable for industrial production, and avoids application limitations caused by the His-tagged peptide.
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Figure CN119613535B_ABST
Abstract
This invention discloses a method for purifying elastin-like proteins based on bioengineering, comprising the following steps: 1) obtaining engineered bacterial cells expressing elastin-like proteins, resuspending the cells in buffer to obtain a bacterial resuspension; 2) adding lysozyme and DNase to the bacterial resuspension, heating to 35–55°C, and stirring for 0.5–2 hours to obtain a bacterial lysate; 3) rapidly cooling to 2–10°C and centrifuging to obtain a clear supernatant; 4) purifying the supernatant by cation exchange chromatography to obtain a protein solution; 5) desalting the protein solution by ultrafiltration to obtain a pure protein aqueous solution; 6) lyophilizing to obtain the protein. This invention achieves pure protein through two purification steps via thermal lysis, improving protein recovery efficiency, reducing production costs, and simultaneously realizing the efficient purification of K proteins independent of His-tagged peptides, making it suitable for industrial production.
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