Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes
Gallic acid and quercetin equivalent were determined in the crude extract of matured leaves Aquilaria malaccensis and Aquilaria subintegra. The leaves of both Aquilaria species were dried at 60 °C for 24 hours, ground and sieved into particle size of 250, 300, 400, 500, and 1000 µm. Then, each parti...
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| Format: | Article |
| Language: | English |
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Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)
2020-12-01
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| Series: | Bulletin of Chemical Reaction Engineering & Catalysis |
| Subjects: | |
| Online Access: | https://journal.bcrec.id/index.php/bcrec/article/view/8864 |
| _version_ | 1797677833725673472 |
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| author | Miradatul Najwa Muhd Rodhi Fazlena Hamzah Ku Halim Ku Hamid |
| author_facet | Miradatul Najwa Muhd Rodhi Fazlena Hamzah Ku Halim Ku Hamid |
| author_sort | Miradatul Najwa Muhd Rodhi |
| collection | DOAJ |
| description | Gallic acid and quercetin equivalent were determined in the crude extract of matured leaves Aquilaria malaccensis and Aquilaria subintegra. The leaves of both Aquilaria species were dried at 60 °C for 24 hours, ground and sieved into particle size of 250, 300, 400, 500, and 1000 µm. Then, each particle size of leaves was soaked in distilled water with a ratio of 1:100 (w/v) for 24 hours and undergoes the pre-treatment method by using ultrasonicator (37 kHz), at the temperature of 60 °C for 30 minutes. The crude extracts were obtained after about 4 hours of hydrodistillation process. The highest concentration of gallic acid and quercetin equivalent was determined in the crude extract from the particle size of 250 µm. The kinetics of pancreatic lipase inhibition was further studied based using the Lineweaver-Burk plot, wherein the concentration of p-NPP as the substrate and pancreatic lipase were varied. Based on the formation of the lines in the plot, the crude leaves extract of both Aquilaria species exhibit the mixed-inhibition on pancreatic lipase, which indicates that in the reaction, the inhibitors were not only attached to the free pancreatic lipase, but also to the pancreatic lipase-(p-NPP) complex. The reaction mechanism was similar to non-competitive inhibition; however the value of dissociation constant, Ki, for both inhibition pathways was different. The inhibition shows an increment in Michaelis-Menten constant (Km) and a reduction in the maximum pancreatic lipase activity (Vm) compared to the reaction without Aquilaria spp. crude extracts (control). This proved that the inhibition occurred in this reaction. Copyright © 2021 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). |
| first_indexed | 2024-03-11T22:50:52Z |
| format | Article |
| id | doaj.art-8ffb27944580428b95b99620748d70e3 |
| institution | Directory Open Access Journal |
| issn | 1978-2993 |
| language | English |
| last_indexed | 2024-03-11T22:50:52Z |
| publishDate | 2020-12-01 |
| publisher | Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS) |
| record_format | Article |
| series | Bulletin of Chemical Reaction Engineering & Catalysis |
| spelling | doaj.art-8ffb27944580428b95b99620748d70e32023-09-22T03:39:13ZengMasyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)Bulletin of Chemical Reaction Engineering & Catalysis1978-29932020-12-0115381882810.9767/bcrec.15.3.8864.818-8284205Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle SizesMiradatul Najwa Muhd Rodhi0https://orcid.org/0000-0001-5175-2980Fazlena Hamzah1Ku Halim Ku Hamid2Faculty of Chemical Engineering, Universiti Teknologi MARA (UiTM), 40450 Shah Alam, Selangor, MalaysiaFaculty of Chemical Engineering, Universiti Teknologi MARA (UiTM), 40450 Shah Alam, Selangor, MalaysiaFaculty of Chemical Engineering, Universiti Teknologi MARA (UiTM), 40450 Shah Alam, Selangor, MalaysiaGallic acid and quercetin equivalent were determined in the crude extract of matured leaves Aquilaria malaccensis and Aquilaria subintegra. The leaves of both Aquilaria species were dried at 60 °C for 24 hours, ground and sieved into particle size of 250, 300, 400, 500, and 1000 µm. Then, each particle size of leaves was soaked in distilled water with a ratio of 1:100 (w/v) for 24 hours and undergoes the pre-treatment method by using ultrasonicator (37 kHz), at the temperature of 60 °C for 30 minutes. The crude extracts were obtained after about 4 hours of hydrodistillation process. The highest concentration of gallic acid and quercetin equivalent was determined in the crude extract from the particle size of 250 µm. The kinetics of pancreatic lipase inhibition was further studied based using the Lineweaver-Burk plot, wherein the concentration of p-NPP as the substrate and pancreatic lipase were varied. Based on the formation of the lines in the plot, the crude leaves extract of both Aquilaria species exhibit the mixed-inhibition on pancreatic lipase, which indicates that in the reaction, the inhibitors were not only attached to the free pancreatic lipase, but also to the pancreatic lipase-(p-NPP) complex. The reaction mechanism was similar to non-competitive inhibition; however the value of dissociation constant, Ki, for both inhibition pathways was different. The inhibition shows an increment in Michaelis-Menten constant (Km) and a reduction in the maximum pancreatic lipase activity (Vm) compared to the reaction without Aquilaria spp. crude extracts (control). This proved that the inhibition occurred in this reaction. Copyright © 2021 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).https://journal.bcrec.id/index.php/bcrec/article/view/8864aquilariagallic acidkinetic inhibitionpancreatic lipasequercetin |
| spellingShingle | Miradatul Najwa Muhd Rodhi Fazlena Hamzah Ku Halim Ku Hamid Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes Bulletin of Chemical Reaction Engineering & Catalysis aquilaria gallic acid kinetic inhibition pancreatic lipase quercetin |
| title | Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes |
| title_full | Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes |
| title_fullStr | Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes |
| title_full_unstemmed | Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes |
| title_short | Kinetic Behaviour of Pancreatic Lipase Inhibition by Ultrasonicated A. malaccensis and A. subintegra Leaves of Different Particle Sizes |
| title_sort | kinetic behaviour of pancreatic lipase inhibition by ultrasonicated a malaccensis and a subintegra leaves of different particle sizes |
| topic | aquilaria gallic acid kinetic inhibition pancreatic lipase quercetin |
| url | https://journal.bcrec.id/index.php/bcrec/article/view/8864 |
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