Evaluation of pancreatin stability through enzyme activity determination
Pancreatin is a biotechnological product containing an enzyme complex, obtained from porcine pancreas, that is employed in treating pancreatic diseases. Experiments regarding the stability of the pharmaceutical formulation containing pancreatin were performed using standard binary mixtures with 6 ex...
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| Format: | Article |
| Language: | English |
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Sciendo
2016-09-01
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| Series: | Acta Pharmaceutica |
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| Online Access: | https://doi.org/10.1515/acph-2016-0037 |
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| _version_ | 1832572664052449280 |
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| author | Terra Gleysson De Paula Vinícius De Farias Marcus Trevisan Marcello Garcia Garcia Jerusa Simone |
| author_facet | Terra Gleysson De Paula Vinícius De Farias Marcus Trevisan Marcello Garcia Garcia Jerusa Simone |
| author_sort | Terra Gleysson De Paula |
| collection | DOAJ |
| description | Pancreatin is a biotechnological product containing an enzyme complex, obtained from porcine pancreas, that is employed in treating pancreatic diseases. Experiments regarding the stability of the pharmaceutical formulation containing pancreatin were performed using standard binary mixtures with 6 excipients in a 1:1 ratio (m/m) and a commercial formulation. To accomplish these goals, samples were stored for 1, 3 and 6 months at 40 ± 1 °C and 75 ± 5 % relative humidity (RH) and 40 ± 1 °C and 0 % RH. Stress testing was also performed. All samples were analyzed to evaluate the α-amylase, lipase and protease activities through UV/Vis spectrophotometry. The results revealed that the excipient proprieties and the storage conditions affected enzyme stability. Humidity was a strong influencing factor in the reduction of α-amylase and protease activities. Stress testing indicated that pH 9.0 and UV light did not induce substantial alterations in enzyme activity. |
| format | Article |
| id | doaj-art-0b19a2eda9be48678336cd7c57e698e9 |
| institution | Kabale University |
| issn | 1846-9558 |
| language | English |
| publishDate | 2016-09-01 |
| publisher | Sciendo |
| record_format | Article |
| series | Acta Pharmaceutica |
| spelling | doaj-art-0b19a2eda9be48678336cd7c57e698e92025-02-02T08:32:25ZengSciendoActa Pharmaceutica1846-95582016-09-0166342343110.1515/acph-2016-0037acph-2016-0037Evaluation of pancreatin stability through enzyme activity determinationTerra Gleysson De Paula0Vinícius De Farias Marcus1Trevisan Marcello Garcia2Garcia Jerusa Simone3Federal University of Alfenas – UNIFAL-MG, Institute of Chemistry Laboratory of Analysis and Characterization of Pharmaceuticals Alfenas, Minas Gerais, BrazilFederal University of Alfenas – UNIFAL-MG, Institute of Chemistry Laboratory of Analysis and Characterization of Pharmaceuticals Alfenas, Minas Gerais, BrazilFederal University of Alfenas – UNIFAL-MG, Institute of Chemistry Laboratory of Analysis and Characterization of Pharmaceuticals Alfenas, Minas Gerais, BrazilFederal University of Alfenas – UNIFAL-MG, Institute of Chemistry Laboratory of Analysis and Characterization of Pharmaceuticals Alfenas, Minas Gerais, BrazilPancreatin is a biotechnological product containing an enzyme complex, obtained from porcine pancreas, that is employed in treating pancreatic diseases. Experiments regarding the stability of the pharmaceutical formulation containing pancreatin were performed using standard binary mixtures with 6 excipients in a 1:1 ratio (m/m) and a commercial formulation. To accomplish these goals, samples were stored for 1, 3 and 6 months at 40 ± 1 °C and 75 ± 5 % relative humidity (RH) and 40 ± 1 °C and 0 % RH. Stress testing was also performed. All samples were analyzed to evaluate the α-amylase, lipase and protease activities through UV/Vis spectrophotometry. The results revealed that the excipient proprieties and the storage conditions affected enzyme stability. Humidity was a strong influencing factor in the reduction of α-amylase and protease activities. Stress testing indicated that pH 9.0 and UV light did not induce substantial alterations in enzyme activity.https://doi.org/10.1515/acph-2016-0037α-amylaselipaseproteasestress testingpancreatin stabilitybiopharmaceuticaluv/vis spectrophotometry |
| spellingShingle | Terra Gleysson De Paula Vinícius De Farias Marcus Trevisan Marcello Garcia Garcia Jerusa Simone Evaluation of pancreatin stability through enzyme activity determination Acta Pharmaceutica α-amylase lipase protease stress testing pancreatin stability biopharmaceutical uv/vis spectrophotometry |
| title | Evaluation of pancreatin stability through enzyme activity determination |
| title_full | Evaluation of pancreatin stability through enzyme activity determination |
| title_fullStr | Evaluation of pancreatin stability through enzyme activity determination |
| title_full_unstemmed | Evaluation of pancreatin stability through enzyme activity determination |
| title_short | Evaluation of pancreatin stability through enzyme activity determination |
| title_sort | evaluation of pancreatin stability through enzyme activity determination |
| topic | α-amylase lipase protease stress testing pancreatin stability biopharmaceutical uv/vis spectrophotometry |
| url | https://doi.org/10.1515/acph-2016-0037 |
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