Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction
Owing to high production cost and low reaction yield, immobilized lipase is rarely used in industrial glycerolysis. This research characterizes the performance of lipase immobilized on rice husk in glycerolysis reaction. By utilizing hexamethylenediamine (HMDA) and glutaraldehyde (GA) as coupling ag...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024
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| Online Access: | http://psasir.upm.edu.my/id/eprint/113250/ http://psasir.upm.edu.my/id/eprint/113250/1/113250.pdf |
| _version_ | 1848866171059699712 |
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| author | Cieh, Ng Lin Mokhtar, Mohd Noriznan Baharuddin, Azhari Samsu Mohammed, Mohd Afandi P. Nor, Mohd Zuhair Mohd Wakisaka, Minato |
| author_facet | Cieh, Ng Lin Mokhtar, Mohd Noriznan Baharuddin, Azhari Samsu Mohammed, Mohd Afandi P. Nor, Mohd Zuhair Mohd Wakisaka, Minato |
| author_sort | Cieh, Ng Lin |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Owing to high production cost and low reaction yield, immobilized lipase is rarely used in industrial glycerolysis. This research characterizes the performance of lipase immobilized on rice husk in glycerolysis reaction. By utilizing hexamethylenediamine (HMDA) and glutaraldehyde (GA) as coupling agents, lipase from Thermomyces lanuginosus was immobilized on oxidized rice husk (ORH). For comparison, another sample was prepared where the lipase was directly immobilized on ORH without the use of HMDA and GA. Then, monoglyceride production was performed via glycerolysis using the immobilized lipase. The FTIR analysis verify interactions on rice husk including rice husk oxidation, HMDA coupling, GA activation and lipase immobilization on rice husk. The study found that within the examined range of added lipase for immobilization (10–40 mg-protein/g-support), ORH–HMDA–GA–Lipase possessed superior outcomes in terms of protein loading, immobilization yield, and recovered glycerolysis activity compared to ORH–Lipase. Besides, ORH–HMDA–GA–Lipase exhibits better storage stability (60°C, 44.9 %) and higher reusability (90.0 % monoglyceride yield at the 8th cycle) against ORH–Lipase. The results confirm satisfying performance of the prepared immobilized lipase in glycerolysis and highlight its enhancements facilitated by coupling agents. |
| first_indexed | 2025-11-15T14:16:21Z |
| format | Article |
| id | upm-113250 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T14:16:21Z |
| publishDate | 2024 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1132502024-11-19T08:06:23Z http://psasir.upm.edu.my/id/eprint/113250/ Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction Cieh, Ng Lin Mokhtar, Mohd Noriznan Baharuddin, Azhari Samsu Mohammed, Mohd Afandi P. Nor, Mohd Zuhair Mohd Wakisaka, Minato Owing to high production cost and low reaction yield, immobilized lipase is rarely used in industrial glycerolysis. This research characterizes the performance of lipase immobilized on rice husk in glycerolysis reaction. By utilizing hexamethylenediamine (HMDA) and glutaraldehyde (GA) as coupling agents, lipase from Thermomyces lanuginosus was immobilized on oxidized rice husk (ORH). For comparison, another sample was prepared where the lipase was directly immobilized on ORH without the use of HMDA and GA. Then, monoglyceride production was performed via glycerolysis using the immobilized lipase. The FTIR analysis verify interactions on rice husk including rice husk oxidation, HMDA coupling, GA activation and lipase immobilization on rice husk. The study found that within the examined range of added lipase for immobilization (10–40 mg-protein/g-support), ORH–HMDA–GA–Lipase possessed superior outcomes in terms of protein loading, immobilization yield, and recovered glycerolysis activity compared to ORH–Lipase. Besides, ORH–HMDA–GA–Lipase exhibits better storage stability (60°C, 44.9 %) and higher reusability (90.0 % monoglyceride yield at the 8th cycle) against ORH–Lipase. The results confirm satisfying performance of the prepared immobilized lipase in glycerolysis and highlight its enhancements facilitated by coupling agents. Elsevier 2024 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/113250/1/113250.pdf Cieh, Ng Lin and Mokhtar, Mohd Noriznan and Baharuddin, Azhari Samsu and Mohammed, Mohd Afandi P. and Nor, Mohd Zuhair Mohd and Wakisaka, Minato (2024) Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction. Biochemical Engineering Journal, 212. art. no. 109500. pp. 1-11. ISSN 1369-703X; eISSN: 1873-295X https://www.sciencedirect.com/science/article/pii/S1369703X24002870 10.1016/j.bej.2024.109500 |
| spellingShingle | Cieh, Ng Lin Mokhtar, Mohd Noriznan Baharuddin, Azhari Samsu Mohammed, Mohd Afandi P. Nor, Mohd Zuhair Mohd Wakisaka, Minato Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title | Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title_full | Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title_fullStr | Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title_full_unstemmed | Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title_short | Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| title_sort | evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction |
| url | http://psasir.upm.edu.my/id/eprint/113250/ http://psasir.upm.edu.my/id/eprint/113250/ http://psasir.upm.edu.my/id/eprint/113250/ http://psasir.upm.edu.my/id/eprint/113250/1/113250.pdf |