Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate
Lipase (E.C 3.1.1.3, triacylglycerol hydrolase) is an important enzyme in biotechnological industries since a lot of applications in food, dairy, detergent, pulp, and pharmaceutical industries. Thermophilic microorganism, Geobacillus vulgivagus dYTae-14, isolated from hot spring in Indonesia, showed...
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id-itb.:119492017-09-27T11:42:37ZIsolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate RESDIA MEGASARI (NIM 10505082), CITRA Indonesia Final Project INSTITUT TEKNOLOGI BANDUNG https://digilib.itb.ac.id/gdl/view/11949 Lipase (E.C 3.1.1.3, triacylglycerol hydrolase) is an important enzyme in biotechnological industries since a lot of applications in food, dairy, detergent, pulp, and pharmaceutical industries. Thermophilic microorganism, Geobacillus vulgivagus dYTae-14, isolated from hot spring in Indonesia, showed an extracellular lipase activity on lipid substrates at high temperature. On olive oil (1.5%, w/v) as a sole carbon source, the isolate dYTae-14 grew very rapidly at 70oC and showed maximum lipase activity at late exponential phase, the activity slowly decrease up to stationary phase. The excreted lipase of dYTae-14 was partially purified by ammonium sulfate fractionation to give 4 fractions, 0-30%, 30-80%, 80-100%, and 100% fractions. Fraction of 0-30% showed the highest activity by using para-nitrophenyl palmitate as substrate. The partial purified enzyme showed optimal activity at 65oC and pH 8. <br /> <br /> text |
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Lipase (E.C 3.1.1.3, triacylglycerol hydrolase) is an important enzyme in biotechnological industries since a lot of applications in food, dairy, detergent, pulp, and pharmaceutical industries. Thermophilic microorganism, Geobacillus vulgivagus dYTae-14, isolated from hot spring in Indonesia, showed an extracellular lipase activity on lipid substrates at high temperature. On olive oil (1.5%, w/v) as a sole carbon source, the isolate dYTae-14 grew very rapidly at 70oC and showed maximum lipase activity at late exponential phase, the activity slowly decrease up to stationary phase. The excreted lipase of dYTae-14 was partially purified by ammonium sulfate fractionation to give 4 fractions, 0-30%, 30-80%, 80-100%, and 100% fractions. Fraction of 0-30% showed the highest activity by using para-nitrophenyl palmitate as substrate. The partial purified enzyme showed optimal activity at 65oC and pH 8. <br />
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Final Project |
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RESDIA MEGASARI (NIM 10505082), CITRA |
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RESDIA MEGASARI (NIM 10505082), CITRA Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
author_facet |
RESDIA MEGASARI (NIM 10505082), CITRA |
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RESDIA MEGASARI (NIM 10505082), CITRA |
title |
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
title_short |
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
title_full |
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
title_fullStr |
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
title_full_unstemmed |
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate |
title_sort |
isolation, purification, and characterization of thermostable lipase from thermophilic bacteria local isolate |
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https://digilib.itb.ac.id/gdl/view/11949 |
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