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Title: | Purification and characterization of a cathepsin inhibitor from catfish (Pangasius sp.) of Indonesian water |
Authors: | Nurhayati, T Rusyadi, S Suwandi, R Nugraha, R |
Issue Date: | 2013 |
Publisher: | IFRJ, Faculty of Food Science & Technology, UPM |
Series/Report no.: | 20(2): 941-946; |
Abstract: | Cathepsin inhibitor has been purified to homogeneity from catfish muscle (Pangasius sp.). The purification was carried out through ammonium sulphate precipitation, followed by ion exchange chromatography using DEAE-Sephadex A-75, followed by gel filtration on Sephadex G-100. Throughout the purification procedure, cathepsin inhibitory activity was determined against hemoglobin. A single band of molecular weight 16.65 kDa was obtained after the Sephadex G-100 filtration and revealed inhibitory activity against cathepsin as estimated by SDS-PAGE. The purified inhibitor possessed a specific activity of 16.9-fold higher than the initial activity with a 1.85 % yield. The optimum pH of the inhibitor was eight at 40°C. The inhibitor was stable at 10-50°C and at pH 7-9. Ions Mn2+ increased the inhibitory activity, while Ca2+ and Co2+ were slightly repressed. The enzyme inhibitor extracted from this study had similar properties to available commercial inhibitors. |
URI: | http://repository.ipb.ac.id/handle/123456789/77145 |
ISSN: | 19854668 |
Appears in Collections: | Faculty of Fisheries and Marine Science |
Files in This Item:
File | Size | Format | |
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IFRJ_2013_Vol.20No.2_941-946.pdf.pdf | 664.45 kB | Adobe PDF | View/Open |
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