Evaluation on potential application of lipase immobilized on rice husks in enzymatic glycerolysis reaction

IF 3.7 3区 生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Biochemical Engineering Journal Pub Date : 2024-09-17 DOI:10.1016/j.bej.2024.109500
Ng Lin Cieh , Mohd Noriznan Mokhtar , Azhari Samsu Baharuddin , Mohd Afandi P. Mohammed , Mohd Zuhair Mohd Nor , Minato Wakisaka
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Abstract

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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评估固定在稻壳上的脂肪酶在酶解甘油反应中的应用潜力
由于生产成本高、反应产率低,固定化脂肪酶很少用于工业甘油分解。本研究表征了固定在稻壳上的脂肪酶在甘油分解反应中的性能。通过使用六亚甲基二胺(HMDA)和戊二醛(GA)作为偶联剂,将来自嗜热酵母菌(Thermomyces lanuginosus)的脂肪酶固定在氧化稻壳(ORH)上。为了进行比较,还制备了另一种样品,将脂肪酶直接固定在 ORH 上,而不使用 HMDA 和 GA。然后,使用固定化脂肪酶通过甘油分解生产单甘酯。傅立叶变换红外分析验证了稻壳上的相互作用,包括稻壳氧化、HMDA偶联、GA活化和脂肪酶固定在稻壳上。研究发现,在所考察的固定化脂肪酶添加量范围内(10-40 毫克蛋白/克-支持物),ORH-HMDA-GA-脂肪酶在蛋白负载量、固定化产量和甘油分解活性恢复方面均优于 ORH-脂肪酶。此外,与 ORH-脂肪酶相比,ORH-HMDA-GA-脂肪酶具有更好的储存稳定性(60°C,44.9%)和更高的可重复使用性(第 8 个周期的单甘油酯产量为 90.0%)。这些结果证实了所制备的固定化脂肪酶在甘油分解方面具有令人满意的性能,并强调了偶联剂对其性能的促进作用。
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来源期刊
Biochemical Engineering Journal
Biochemical Engineering Journal 工程技术-工程:化工
CiteScore
7.10
自引率
5.10%
发文量
380
审稿时长
34 days
期刊介绍: The Biochemical Engineering Journal aims to promote progress in the crucial chemical engineering aspects of the development of biological processes associated with everything from raw materials preparation to product recovery relevant to industries as diverse as medical/healthcare, industrial biotechnology, and environmental biotechnology. The Journal welcomes full length original research papers, short communications, and review papers* in the following research fields: Biocatalysis (enzyme or microbial) and biotransformations, including immobilized biocatalyst preparation and kinetics Biosensors and Biodevices including biofabrication and novel fuel cell development Bioseparations including scale-up and protein refolding/renaturation Environmental Bioengineering including bioconversion, bioremediation, and microbial fuel cells Bioreactor Systems including characterization, optimization and scale-up Bioresources and Biorefinery Engineering including biomass conversion, biofuels, bioenergy, and optimization Industrial Biotechnology including specialty chemicals, platform chemicals and neutraceuticals Biomaterials and Tissue Engineering including bioartificial organs, cell encapsulation, and controlled release Cell Culture Engineering (plant, animal or insect cells) including viral vectors, monoclonal antibodies, recombinant proteins, vaccines, and secondary metabolites Cell Therapies and Stem Cells including pluripotent, mesenchymal and hematopoietic stem cells; immunotherapies; tissue-specific differentiation; and cryopreservation Metabolic Engineering, Systems and Synthetic Biology including OMICS, bioinformatics, in silico biology, and metabolic flux analysis Protein Engineering including enzyme engineering and directed evolution.
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