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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Main Author: RESDIA MEGASARI (NIM 10505082), CITRA
Format: Final Project
Language:Indonesia
Online Access:https://digilib.itb.ac.id/gdl/view/11949
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Institution: Institut Teknologi Bandung
Language: Indonesia
id id-itb.:11949
spelling 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
institution Institut Teknologi Bandung
building Institut Teknologi Bandung Library
continent Asia
country Indonesia
Indonesia
content_provider Institut Teknologi Bandung
collection Digital ITB
language Indonesia
description 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 />
format Final Project
author RESDIA MEGASARI (NIM 10505082), CITRA
spellingShingle RESDIA MEGASARI (NIM 10505082), CITRA
Isolation, Purification, and Characterization of Thermostable Lipase from Thermophilic Bacteria Local Isolate
author_facet RESDIA MEGASARI (NIM 10505082), CITRA
author_sort 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
url https://digilib.itb.ac.id/gdl/view/11949
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