Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization
Native lipase is still promising as an industrial biocatalyst. This study aimed to investigate the production of native local lipase using solid state fermentation (SSF) methods, immobilization the lipase by Ca-alginate entrapment, and characterization based on substrate preferences. To obtain high...
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Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)
2024-12-01
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| Series: | Bulletin of Chemical Reaction Engineering & Catalysis |
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| Online Access: | https://journal.bcrec.id/index.php/bcrec/article/view/20234 |
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| author | Titin Haryati Norman Yoshi Haryono Dian Nugraheni Fenti Fatmawati Alfina Kusuma Dewi Muhammad Zahran Edlian Syach |
| author_facet | Titin Haryati Norman Yoshi Haryono Dian Nugraheni Fenti Fatmawati Alfina Kusuma Dewi Muhammad Zahran Edlian Syach |
| author_sort | Titin Haryati |
| collection | DOAJ |
| description | Native lipase is still promising as an industrial biocatalyst. This study aimed to investigate the production of native local lipase using solid state fermentation (SSF) methods, immobilization the lipase by Ca-alginate entrapment, and characterization based on substrate preferences. To obtain high lipase production using SSF methods, we optimized the type of agro-wastes substrates, fermentation time, oil induction percentage and volume of preculture percentage. The optimal condition for lipase production via solid-state fermentation involved a 7% (v/v) preculture of Pseudomonas aeruginosa SB-37, utilizing palm kernel meal as the substrate, supplemented with 6% (v/w) oil induction (soybean oil:tween 80 = 75:25) at 50 °C for 24 h. This gave a lypolitic activity value of 2 U/gds (gram dry weight substrates). Since the protein profile of extracellular lipase has a few protein bands, we perform direct immobilization on crude protein supernatant. Immobilization by Ca-alginate entrapment results in loading capacity and recovery activity values of 86.84% and 148%, respectively. The immobilized lipase retained 92% activity until four batch repetition and keep 40% activity at tenth batch. The highest hydrolytic activity of immobilized lipase was 0.9 U/g gel on the pNP_8 substrates. While the highest transesterification activity was observed with acetonitrile solvent and substrates of pNP_8 and isopropanol with the activity value at 0.6 U/g gel. This present study emphasized the feasibility of producing lipase as a biocatalysts using economical agro-industrial wastes and efficient immobilization using entrapment method. Copyright © 2024 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0). |
| format | Article |
| id | doaj-art-ad37b7cde95f450db0af9291a4bac38c |
| institution | Kabale University |
| issn | 1978-2993 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS) |
| record_format | Article |
| series | Bulletin of Chemical Reaction Engineering & Catalysis |
| spelling | doaj-art-ad37b7cde95f450db0af9291a4bac38c2025-02-02T02:54:01ZengMasyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)Bulletin of Chemical Reaction Engineering & Catalysis1978-29932024-12-0119471072110.9767/bcrec.202348485Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and CharacterizationTitin Haryati0https://orcid.org/0000-0002-4390-4128Norman Yoshi Haryono1Dian Nugraheni2Fenti Fatmawati3Alfina Kusuma Dewi4Muhammad Zahran Edlian Syach5Research Center for Applied Microbiology, National Research and Innovation Agency, Jalan Raya Bogor KM 46, Cibinong, Bogor, 16911, West Java, IndonesiaBiotechnology Study Program, Department of Applied Science, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, Jl. Semarang No. 5, Malang 65145, IndonesiaBhakti Kencana University, Jalan Soekarno Hatta No.754, Cipadung Kidul, Bandung, 40614, West Java, IndonesiaBhakti Kencana University, Jalan Soekarno Hatta No.754, Cipadung Kidul, Bandung, 40614, West Java, IndonesiaBiotechnology Study Program, Department of Applied Science, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, Jl. Semarang No. 5, Malang 65145, IndonesiaBiotechnology Study Program, Department of Applied Science, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, Jl. Semarang No. 5, Malang 65145, IndonesiaNative lipase is still promising as an industrial biocatalyst. This study aimed to investigate the production of native local lipase using solid state fermentation (SSF) methods, immobilization the lipase by Ca-alginate entrapment, and characterization based on substrate preferences. To obtain high lipase production using SSF methods, we optimized the type of agro-wastes substrates, fermentation time, oil induction percentage and volume of preculture percentage. The optimal condition for lipase production via solid-state fermentation involved a 7% (v/v) preculture of Pseudomonas aeruginosa SB-37, utilizing palm kernel meal as the substrate, supplemented with 6% (v/w) oil induction (soybean oil:tween 80 = 75:25) at 50 °C for 24 h. This gave a lypolitic activity value of 2 U/gds (gram dry weight substrates). Since the protein profile of extracellular lipase has a few protein bands, we perform direct immobilization on crude protein supernatant. Immobilization by Ca-alginate entrapment results in loading capacity and recovery activity values of 86.84% and 148%, respectively. The immobilized lipase retained 92% activity until four batch repetition and keep 40% activity at tenth batch. The highest hydrolytic activity of immobilized lipase was 0.9 U/g gel on the pNP_8 substrates. While the highest transesterification activity was observed with acetonitrile solvent and substrates of pNP_8 and isopropanol with the activity value at 0.6 U/g gel. This present study emphasized the feasibility of producing lipase as a biocatalysts using economical agro-industrial wastes and efficient immobilization using entrapment method. Copyright © 2024 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).https://journal.bcrec.id/index.php/bcrec/article/view/20234native lipasessfagrowastespalm kernel mealalginate entrapment |
| spellingShingle | Titin Haryati Norman Yoshi Haryono Dian Nugraheni Fenti Fatmawati Alfina Kusuma Dewi Muhammad Zahran Edlian Syach Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization Bulletin of Chemical Reaction Engineering & Catalysis native lipase ssf agrowastes palm kernel meal alginate entrapment |
| title | Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization |
| title_full | Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization |
| title_fullStr | Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization |
| title_full_unstemmed | Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization |
| title_short | Extracellular Lipase from Pseudomonas aeruginosa SB-37: Production by Solid State Fermentation, Immobilization, and Characterization |
| title_sort | extracellular lipase from pseudomonas aeruginosa sb 37 production by solid state fermentation immobilization and characterization |
| topic | native lipase ssf agrowastes palm kernel meal alginate entrapment |
| url | https://journal.bcrec.id/index.php/bcrec/article/view/20234 |
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