Liguang Zhang, Yanan Shen, Wenjing Lu, Lengqiu Guo, Min Xiang and Dayong Zhang* Pages 741 - 747 ( 7 )
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.Methods: 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. Results: 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.
Dry film, ethylene glycol, gelatin film, β-glucosidase, protein stabilization, SEM.
College of Pharmacy, Suzhou Vocational Health College, Suzhou, School of Pharmacy, Xuzhou Medicinal University, Xuzhou, College of Pharmacy, Suzhou Vocational Health College, Suzhou, College of Pharmacy, Suzhou Vocational Health College, Suzhou, College of Pharmacy, Suzhou Vocational Health College, Suzhou, State Key Laboratory of Crop Genetics & Germplasm Enhancement, Nanjing Agricultural University, Nanjing