Background:
Although the stability of proteins is of significance to maintain protein function
for therapeutical applications, this remains a challenge. Herein, a general method of preserving
protein stability and function was developed using gelatin films.
Method:
Enzymes immobilized onto films composed of gelatin and Ethylene Glycol (EG) were developed
to study their ability to stabilize proteins. As a model functional protein, β-glucosidase was selected.
The tensile properties, microstructure, and crystallization behavior of the gelatin films were assessed.
Result:
Our results indicated that film configurations can preserve the activity of β-glucosidase under
rigorous conditions (75% relative humidity and 37°C for 47 days). In both control films and films containing
1.8 % β-glucosidase, tensile strength increased with increased EG content, whilst the elongation
at break increased initially, then decreased over time. The presence of β-glucosidase had a negligible
influence on tensile strength and elongation at break. Scanning electron-microscopy (SEM) revealed
that with increasing EG content or decreasing enzyme concentrations, a denser microstructure
was observed.
Conclusion:
In conclusion, the dry film is a promising candidate to maintain protein stabilization and
handling. The configuration is convenient and cheap, and thus applicable to protein storage and transportation
processes in the future.
Monomer‐scale design of functional protein polymers using consensus repeat sequences
