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通过离子液体修饰的 FeO 载体固定化实现脂肪酶的快速分离和酶学性能的提高。

Quick separation and enzymatic performance improvement of lipase by ionic liquid-modified FeO carrier immobilization.

机构信息

School of Food and Biological Engineering, Jiangsu University, No. 301 Xuefu Road, Zhenjiang, 212013, China.

出版信息

Bioprocess Biosyst Eng. 2018 May;41(5):739-748. doi: 10.1007/s00449-018-1907-2. Epub 2018 Feb 6.

DOI:10.1007/s00449-018-1907-2
PMID:29411098
Abstract

To promote the activity and stability of immobilized porcine pancreatic lipase (PPL), novel carrier was combined with special immobilization method. Enzymatic activity was enhanced after immobilized onto ionic liquid modified magnetic FeO by electrostatic adsorption. Activity of immobilized enzyme (PPL-IM/BF-FeO@CA) reached 596 U/g PPL. Through the combination of electrostatic adsorption and embedding immobilization methods, we improve binding force between the carrier and enzyme, and further enhance the efficiency and stability of immobilized enzyme. The activity of PPL-IM/BF-FeO@CA after repeated third use was 78%. After storage at room temperature for 5 days, the residual activity was 89%. Enzymatic properties and catalytic kinetics of immobilized enzymes were studied, and the effect mechanism of ionic liquid modified FeO on PPL was revealed. The effect of ionic liquid on the carrier structure was investigated by characterization of XRD, FT-IR, SEM and TG. The mechanism and enzymatic properties of immobilized PPL via electrostatic adsorption and embedding were analyzed. A novel and efficient immobilized PPL was developed.

摘要

为了提高固定化猪胰脂肪酶(PPL)的活性和稳定性,将新型载体与特殊的固定化方法相结合。通过静电吸附将其固定在离子液体修饰的磁性 FeO 上后,酶的活性得到了增强。固定化酶(PPL-IM/BF-FeO@CA)的酶活达到 596 U/g PPL。通过静电吸附和包埋固定化方法的结合,提高了载体与酶之间的结合力,进一步提高了固定化酶的效率和稳定性。第三次重复使用后,PPL-IM/BF-FeO@CA 的活性为 78%。在室温下储存 5 天后,剩余活性为 89%。研究了固定化酶的酶学性质和催化动力学,并揭示了离子液体修饰的 FeO 对 PPL 的作用机制。通过 XRD、FT-IR、SEM 和 TG 对载体结构进行了表征,研究了离子液体对载体结构的影响。通过分析静电吸附和包埋固定化 PPL 的机制和酶学性质,开发了一种新型高效的固定化 PPL。

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