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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...
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Published in: | Biochemical engineering journal 2024-12, Vol.212, p.109500, Article 109500 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | 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.
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•Oxidized rice husk is used as carrier to immobilize Thermomyces lanuginosus lipase.•With the use of coupling agents, the properties of immobilized lipase are improved.•The highest recovered activity achieved was 41.38 %.•Lipase bound with coupling agents is more stable (44.90 %) after 30-day-storage (60 °C).•Lipase immobilized via coupling agents retains 90.00 % yield upon 8 cycles of reaction. |
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ISSN: | 1369-703X |
DOI: | 10.1016/j.bej.2024.109500 |