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Enzymatic methods for in situ cell entrapment and cell release
Tianhong Chen1, David A Small, Martin K McDermott
1Center for Biosystems Research, University of Maryland Biotechnology Institute, 5115 Plant Sciences Building, College Park, Maryland 20742-4450, USA.
Biomacromolecules
|November 11, 2003
Summary
This study introduces an enzyme-based method to entrap E. coli cells in gelatin hydrogels. The method allows rapid cell growth and release, showing promise for biosensor applications.
Area of Science:
- Biotechnology
- Biomaterials Science
- Microbiology
Background:
- Cell encapsulation is crucial for various biotechnological applications.
- Existing methods often require harsh conditions or external triggers.
- Developing mild, in situ cell entrapment techniques is essential.
Purpose of the Study:
- To develop an enzyme-based method for in situ cell entrapment in a hydrogel matrix.
- To investigate the viability and growth of entrapped cells.
- To assess the release of cells from the hydrogel under mild conditions.
Main Methods:
- Utilized a calcium-independent microbial transglutaminase to catalyze gelation of a 10% gelatin solution containing E. coli cells.
- Monitored hydrogel formation and cell growth within the matrix.
- Assessed cell response to induction and release using proteinase K.
Main Results:
- Transglutaminase successfully catalyzed in situ hydrogel formation within 2-3 hours.
- Entrapped E. coli cells exhibited rapid growth and responded to induction.
- Proteinase K rapidly hydrolyzed the hydrogel, releasing viable cells that could be further cultured and induced.
Conclusions:
- Enzyme-mediated in situ cell entrapment in gelatin hydrogels is feasible and efficient.
- This method supports robust cell growth and responsiveness.
- The ability to release viable cells offers significant advantages for applications like microfluidic biosensors.