Engineered Bovine Serum Albumin Nanoparticles Incorporated Alpha Amylase Preparation for the Improved Activity
nano albumin, amylase, nanosphere, enzyme activity
Abstract
In the present study, the improved enzyme activity of alpha amylase encapsulated with bovine serum albumin nanoparticle (BSA) was carried out. Initially. The method for preparation of BSA nanoparticles was optimized with various parameters such as pH, acetone to BSA ratio, cross linking time and concentration of BSA. The optimal pH was found to be 4.5, 10 mg/ml of BSA concentration, acetone to albumin ratio was to be 4.5, cross linking time of 3hrs which gives the higher yield of BSA nanoparticles. The Nano-enzyme conjugate was prepared using the optimized conditions. The encapsulation of α-Amylase Enzyme with BSA Nanoparticle was done based on hydrophobic ion pairing (HIP) complexation. And the Scanning electron micrographs of BSA nanoparticle encapsulated enzyme at the targeted size of 100nm. Distinct changes in the kinetic parameters of nano albumin encapsulated α-amylase was observed. Enzyme activity of nano encapsulated alpha amylase was found to be maximum at the pH of 8.0, temperature 80ºC and 4.5mg/ml of substrate concentration.
Downloads
- Article PDF
- TEI XML Kaleidoscope (download in zip)* (Beta by AI)
- Lens* NISO JATS XML (Beta by AI)
- HTML Kaleidoscope* (Beta by AI)
- DBK XML Kaleidoscope (download in zip)* (Beta by AI)
- LaTeX pdf Kaleidoscope* (Beta by AI)
- EPUB Kaleidoscope* (Beta by AI)
- MD Kaleidoscope* (Beta by AI)
- FO Kaleidoscope* (Beta by AI)
- BIB Kaleidoscope* (Beta by AI)
- LaTeX Kaleidoscope* (Beta by AI)
How to Cite
References
A. Arnedo, S. Espuelas, J. Irache (2002) Albumin nanoparticles as carriers for a phosphodiester oligonucleotide. 1-2.
M. Jahanshahi, G. Najafpour, M. Rahimnejad (2008) Applying the Taguchi method for optimized fabrication of bovine serum albumin (BSA) nanoparticles as drug delivery vehicles. 7(4), 362-367.
K. Langer, S. Balthasar, V. Vogel, N. Dinauer, H. Von Briesen, D. Schubert (2003) Optimization of the preparation process for human serum albumin (HSA) nanoparticles. 257(1-2), 169-180. https://doi.org/10.1016/s0378-5173(03)00134-0
Manisha Desai, Vinod Labhasetwar, Gordon Amidon, Robert Levy (1996) Gastrointestinal Uptake of Biodegradable Microparticles: Effect of Particle Size. 13(12), 1838-1845. https://doi.org/10.1023/a:1016085108889
S. namasivayam, D.nirmala (2011) Enhanced production of alpha amylase using vegetables wastes by aspergillus niger strain SK01 marine isolate. 40(1), 130-133.
V. Prasanna, Aiyer (2005) Aiyer, Amylases and their applications, African Journal of Biotechnology Vol. 4(13), 1525-1529.
Ivo safarik (1989) Rapid detection of alpha amylase inhibitors. 9, 153.
A. Pandey, P. Selvakumar, C. Soccol, P. Nigam (1999) Solid--state fermentation for the production of industrial enzymes. 77, 149-162.
H. Sodhi, K. Sharma, J. Gupta, S. Soni (2005) Production of a thermostable a-amylase from Bacillus sp. PS-7 by solid-state fermentation and its synergistic use in the hydrolysis of malt starch for alcohol production. 40, 525-534.
F. Francis, A. Sabu, K. Nampoothiri, S. Ramachandran, S. Ghosh, G. Szakacs, A. Pandey (2003) Use of response surface methodology for optimizing process parameters for the production of a-amylase by Aspergillus oryzae. 15, 107-115.
P. Vishwanathan, N. Surlikar (2001) Production of aamylase with Aspergillus flavus on Amaranthus grains by solid-state fermentation. 41, 57-64.
G. Muller, H. Leuenberger, T. Kissel (1996) Albumin nanospheres as carriers for passive drug targeting: An optimized manufacturing technique. 13(1), 32-37. https://doi.org/10.1023/a:1016064930502
Gunter Oberdorster, Juraj Ferin, Bruce Lehnert (1994) Correlation between Particle Size, In Vivo Particle Persistence, and Lung Injury. 102(5), 173. https://doi.org/10.2307/3432080
Published
2014-03-04
Issue
Section
License
Copyright (c) 2014 Authors and Global Journals Private Limited
This work is licensed under a Creative Commons Attribution 4.0 International License.