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...

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Published in:Bulletin of Chemical Reaction Engineering & Catalysis
Main Authors: Azianna Gusniah, Harumi Veny, Fazlena Hamzah
Format: Article in Journal/Newspaper
Language:English
Indonesian
Published: Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS) 2020
Subjects:
Online Access:https://doi.org/10.9767/bcrec.15.1.6648.242-252
https://doaj.org/article/cb0f3141a98a467c88a5bfaf61f62335
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spelling 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
institution Open Polar
collection Directory of Open Access Journals: DOAJ Articles
op_collection_id ftdoajarticles
language English
Indonesian
topic enzyme activity
immobilized lipase
transesterifications
waste cooking oil
Chemical engineering
TP155-156
spellingShingle 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
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container_title Bulletin of Chemical Reaction Engineering & Catalysis
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container_start_page 242
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