Evaluation of pancreatin stability through enzyme activity determination

1. R. Noor, N. Zerin and K. K. Das, Microbiological quality of pharmaceutical products in Bangladesh: Current research perspective, Asian Pac. J. Trop. Dis. 5 (2015) 264-270; DOI: 10.1016/s2222-1808(14)60781-7.10.1016/S2222-1808(14)60781-7Search in Google Scholar

2. E. Tamizi and A. Jouyban, Forced degradation studies of biopharmaceuticals: Selection of stress conditions, Eur. J. Pharm. Biopharm. 98 (2016) 26-46; DOI: 10.1016/j.ejpb.2015.10.016.10.1016/j.ejpb.2015.10.01626542454Search in Google Scholar

3. United States Pharmacopeia 32, National Formulary 27, USP Convention, Rockville 2010.Search in Google Scholar

4. A. V. Berdutina, A. D. Neklyudov, A. I. Ivankin, B. S. Karpo and S. I. Mitaleva, Comparison of proteolytic activities of the enzyme complex from mammalian pancreas and pancreatin, Appl. Biochem. Micro. 36 (2000) 363-367.10.1007/BF02738043Search in Google Scholar

5. International Conference on Harmonization of Technical Requirements for Registration of Pharmaceuticals for Human Use, ICH Harmonized Tripartite Guideline, Quality of Biotechnological Products: Stability Testing of Biotechnological/Biological Products Q5C, November 1995.Search in Google Scholar

6. M. Blessy, R. D. Patel, P. N. Prajapati and Y. K. Agrawal, Development of forced degradation and stability indicating studies of drugs - A review, J. Pharm. Anal. 4 (2014) 159-165; DOI: 10.1016/j. jpha.2013.09.003.Search in Google Scholar

7. M. Printz and W. Friess, Simultaneous detection and analysis of protein aggregation and protein unfolding by size exclusion chromatography with post column addition of the fluorescent dye BisANS, J. Pharm. Sci. 101 (2012) 826-837; DOI: 10.1002/jps.22808.10.1002/jps.2280822095720Search in Google Scholar

8. K. Singh and A. M. Kayastha, Amylase from wheat (Triticum aestivun) seeds: its purification, biochemical attributes and active site studies, Food Chem. 162 (2014) 1-9; DOI: 10.1016/j.foodchem.2014.04.043.10.1016/j.foodchem.2014.04.04324874349Search in Google Scholar

9. ANVISA. Resolução da diretoria colegiada - RDC nº 55 de 14 de novembro de 2012; http://portal.anvisa.gov.br/wps/wcm/connect/5b22ac004d9a646fb63ff7c116238c3b/27+de+novembro+RDC+55_2012++Detergentes+Enzimaticos.pdf?MOD=AJPERES; access date March 16, 2015.Search in Google Scholar

10. J. Russell, Measuring amylase activity in cereal grains, J. Res. Meth. 9 (2007) 11-13.Search in Google Scholar

11. S. S. Kanwar, R. K. Kaushal, A. Jawed, R. Gupta and S. S. Chimni, Methods for inhibitions of residual lipase activity in colorimetric assay: A comparative study, Indian J. Biochem. Bio. 42 (2005) 233-237.Search in Google Scholar

12. M. A. Abd-Elhakeem, A. M. Elsayed and T. A. Alkhulaqi, New colorimetric method for lipases Activity assay in microbial media, Am. J. Anal. Chem. 4 (2013) 442-444; DOI: 10.4236/ajac.2013.49055.10.4236/ajac.2013.49055Search in Google Scholar

13. L. Scalvini, D. Piomelli and M. Mor, Monoglyceride lipase: structure and inhibitors, Chem. Phys. Lipids 197 (2016) 13-24; DOI: 10.1016/j.chemphyslip.2015.07.011.10.1016/j.chemphyslip.2015.07.011472805726216043Search in Google Scholar

14. K. C. Waterman, R. C. Adami, K. M. Alsante, J. Hong, M. S. Landis, F. Lombardo and C. J. Roberts, Stabilization of pharmaceuticals to oxidative degradation, Pharm. Dev. Technol. 7 (2002) 1-32; DOI: 10.1081/PDT-120002237.10.1081/PDT-12000223711852692Search in Google Scholar

15. E. Buxbaum, Biophysical Chemistry of Protein. An Introduction to Laboratory Methods, 1st ed., Springer, New York 2011.Search in Google Scholar