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将脂肪酶固定在细菌磁小体上用于去污。

Immobilisation of lipase enzyme onto bacterial magnetosomes for stain removal.

作者信息

Jacob Jobin John, Suthindhiran K

机构信息

Senior Research Fellow-DST, Marine Biotechnology and Bioproducts Laboratory, School of Bio Sciences and Technology, VIT, Vellore, 632014, Tamil Nadu, India.

Marine Biotechnology and Bioproducts Laboratory, School of Bio Sciences and Technology, Vellore Institute of Technology, Vellore, 632014, Tamil Nadu, India.

出版信息

Biotechnol Rep (Amst). 2020 Jan 17;25:e00422. doi: 10.1016/j.btre.2020.e00422. eCollection 2020 Mar.

DOI:10.1016/j.btre.2020.e00422
PMID:31993344
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6976927/
Abstract

Lipase was immobilized onto bacterial magnetosomes using glutaraldehyde cross-linking and confirmed by Fourier transform infrared spectrometry (FT-IR) and Scanning electron microscopy (SEM). Enzyme activity of immobilised lipase as well as free lipase was estimated by the release of p-nitro phenol due to the hydrolysis of -nitro phenyl acetate (pNPA). The immobilisation yield of lipase onto magnetosome was found to be 88 %. The optimal pH (7) and temperature (40 °C) for activity was standardised and found to be similar to free lipase. The stored immobilized lipase maintained higher activity even after 30 days at a temperature of 4 °C whereas compared to free lipase. Immobilized lipase found to have removed vegetable oil stain and showed higher cleaning efficiency when compared to free lipase. The results suggest that bacterial magnetosome displays great potential as a support material for the immobilization of industrial enzymes such as lipase.

摘要

利用戊二醛交联法将脂肪酶固定在细菌磁小体上,并通过傅里叶变换红外光谱(FT - IR)和扫描电子显微镜(SEM)进行了确认。通过对硝基苯乙酸(pNPA)水解产生对硝基苯酚的释放量来估算固定化脂肪酶以及游离脂肪酶的酶活性。发现脂肪酶在磁小体上的固定化产率为88%。将脂肪酶活性的最佳pH(7)和温度(40°C)标准化,发现与游离脂肪酶相似。与游离脂肪酶相比,储存后的固定化脂肪酶即使在4°C下放置30天后仍保持较高活性。发现固定化脂肪酶去除了植物油污渍,与游离脂肪酶相比显示出更高的清洁效率。结果表明,细菌磁小体作为固定化脂肪酶等工业酶的载体材料具有巨大潜力。

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