Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil
Biodiesel is fatty acid methyl ester that commonly derived from vegetable oils and animal fats that can be produced through enzymatic transesterification using lipase. In this study, three different types of lipase were used, which are Lipase Immobilized Pseudomonas cepacia, PcL, Thermomyces lanugin...
Published in: | Bulletin of Chemical Reaction Engineering & Catalysis |
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Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)
2020
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Online Access: | https://doi.org/10.9767/bcrec.15.1.6648.242-252 https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335 |
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ftdoajarticles:oai:doaj.org/article:cb0f3141a98a467c88a5bfaf61f62335 2023-10-09T21:47:09+02:00 Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil Azianna Gusniah Harumi Veny Fazlena Hamzah 2020-04-01T00:00:00Z https://doi.org/10.9767/bcrec.15.1.6648.242-252 https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335 EN ID eng ind Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS) https://journal.bcrec.id/index.php/bcrec/article/view/6648 https://doaj.org/toc/1978-2993 1978-2993 doi:10.9767/bcrec.15.1.6648.242-252 https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335 Bulletin of Chemical Reaction Engineering & Catalysis, Vol 15, Iss 1, Pp 242-252 (2020) enzyme activity immobilized lipase transesterifications waste cooking oil Chemical engineering TP155-156 article 2020 ftdoajarticles https://doi.org/10.9767/bcrec.15.1.6648.242-252 2023-09-24T00:35:32Z Biodiesel is fatty acid methyl ester that commonly derived from vegetable oils and animal fats that can be produced through enzymatic transesterification using lipase. In this study, three different types of lipase were used, which are Lipase Immobilized Pseudomonas cepacia, PcL, Thermomyces lanuginosus, TLIM, and Candida Antarctica A (recombinant from Aspergillus oryzae), CALA. These lipases were compared based on their activity at different pH (6-10), temperature (30-50 °C), activation energy, and amount of lipase loading for hydrolysis of p-NPA into n-NP. The result indicates that among the lipase used in the study, CALA is the preferable biocatalyst in the hydrolysis of p-NPA due to the minimum energy required and higher enzymatic activity at 20 mg of enzyme loading. PcL and CALA used in the study gave the optimum activity at pH 9 except for TLIM at pH 8 and the optimum temperature at 40 °C. The kinetic data obtained for CALA in this reaction were Km = 57.412 mM and Vm = 70 µM/min. This finding shows that CALA is beneficial biocatalysts for the transesterification process to obtain a higher product with lower activation energy. Copyright © 2020 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0). Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Bulletin of Chemical Reaction Engineering & Catalysis 15 1 242 252 |
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enzyme activity immobilized lipase transesterifications waste cooking oil Chemical engineering TP155-156 |
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enzyme activity immobilized lipase transesterifications waste cooking oil Chemical engineering TP155-156 Azianna Gusniah Harumi Veny Fazlena Hamzah Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
topic_facet |
enzyme activity immobilized lipase transesterifications waste cooking oil Chemical engineering TP155-156 |
description |
Biodiesel is fatty acid methyl ester that commonly derived from vegetable oils and animal fats that can be produced through enzymatic transesterification using lipase. In this study, three different types of lipase were used, which are Lipase Immobilized Pseudomonas cepacia, PcL, Thermomyces lanuginosus, TLIM, and Candida Antarctica A (recombinant from Aspergillus oryzae), CALA. These lipases were compared based on their activity at different pH (6-10), temperature (30-50 °C), activation energy, and amount of lipase loading for hydrolysis of p-NPA into n-NP. The result indicates that among the lipase used in the study, CALA is the preferable biocatalyst in the hydrolysis of p-NPA due to the minimum energy required and higher enzymatic activity at 20 mg of enzyme loading. PcL and CALA used in the study gave the optimum activity at pH 9 except for TLIM at pH 8 and the optimum temperature at 40 °C. The kinetic data obtained for CALA in this reaction were Km = 57.412 mM and Vm = 70 µM/min. This finding shows that CALA is beneficial biocatalysts for the transesterification process to obtain a higher product with lower activation energy. Copyright © 2020 by Authors, Published by BCREC Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0). |
format |
Article in Journal/Newspaper |
author |
Azianna Gusniah Harumi Veny Fazlena Hamzah |
author_facet |
Azianna Gusniah Harumi Veny Fazlena Hamzah |
author_sort |
Azianna Gusniah |
title |
Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
title_short |
Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
title_full |
Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
title_fullStr |
Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
title_full_unstemmed |
Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil |
title_sort |
activity and stability of immobilized lipase for utilization in transesterification of waste cooking oil |
publisher |
Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS) |
publishDate |
2020 |
url |
https://doi.org/10.9767/bcrec.15.1.6648.242-252 https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Bulletin of Chemical Reaction Engineering & Catalysis, Vol 15, Iss 1, Pp 242-252 (2020) |
op_relation |
https://journal.bcrec.id/index.php/bcrec/article/view/6648 https://doaj.org/toc/1978-2993 1978-2993 doi:10.9767/bcrec.15.1.6648.242-252 https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335 |
op_doi |
https://doi.org/10.9767/bcrec.15.1.6648.242-252 |
container_title |
Bulletin of Chemical Reaction Engineering & Catalysis |
container_volume |
15 |
container_issue |
1 |
container_start_page |
242 |
op_container_end_page |
252 |
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