PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS
</i><b>Abstract: <i></b><p align=\"justify\"> The phosphatases indicated in this research are phosphomonoesterases, i.e. enzymes that catalyze the hydrolysis of the -P-O- bond of orthophosphoric monoesters and producing ROH and H<sub>3</sub>PO<s...
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id-itb.:45352006-10-05T11:44:52ZPEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS Harliansyah Indonesia Theses INSTITUT TEKNOLOGI BANDUNG https://digilib.itb.ac.id/gdl/view/4535 </i><b>Abstract: <i></b><p align=\"justify\"> The phosphatases indicated in this research are phosphomonoesterases, i.e. enzymes that catalyze the hydrolysis of the -P-O- bond of orthophosphoric monoesters and producing ROH and H<sub>3</sub>PO<sub>4</sub>. These enzymes are widely distributed in living organisms but, until now, the enzyme have not been reported present in pineapple.<p align=\"justify\"> The pineapple phosphatase was extracted, partially purified and characterized, using p-nitrophenyl phosphate as substrate. The result showed that, the enzyme had a pH optimum of 6.0, temperature optimum of 40°C. The Michaelis - Menten constant (Km) and its maximum velocity (Vmax) were 1.87 mM and 2.2452 μmol/min respectively. This pineapple acid phosphatase was not affected by metal ion Mg<sup>++</sup>. text |
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</i><b>Abstract: <i></b><p align=\"justify\"> The phosphatases indicated in this research are phosphomonoesterases, i.e. enzymes that catalyze the hydrolysis of the -P-O- bond of orthophosphoric monoesters and producing ROH and H<sub>3</sub>PO<sub>4</sub>. These enzymes are widely distributed in living organisms but, until now, the enzyme have not been reported present in pineapple.<p align=\"justify\"> The pineapple phosphatase was extracted, partially purified and characterized, using p-nitrophenyl phosphate as substrate. The result showed that, the enzyme had a pH optimum of 6.0, temperature optimum of 40°C. The Michaelis - Menten constant (Km) and its maximum velocity (Vmax) were 1.87 mM and 2.2452 μmol/min respectively. This pineapple acid phosphatase was not affected by metal ion Mg<sup>++</sup>. |
| format |
Theses |
| author |
Harliansyah |
| spellingShingle |
Harliansyah PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| author_facet |
Harliansyah |
| author_sort |
Harliansyah |
| title |
PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| title_short |
PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| title_full |
PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| title_fullStr |
PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| title_full_unstemmed |
PEMURNIAN PARSIAL DAN KARAKTERISASI FOSFATASE ASAM DARI ANANAS COMUSUS |
| title_sort |
pemurnian parsial dan karakterisasi fosfatase asam dari ananas comusus |
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https://digilib.itb.ac.id/gdl/view/4535 |
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