Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe3O4 Nanoparticles

Bi, Yanhong; Wang, Zhaoyu; Zhang, Rui; Diao, Yihan; Tian, Yaoqi; Jin, Zhengyu

doi:10.3390/pr8050629

Open AccessArticle

Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles

by

Yanhong Bi

^1,2,

Zhaoyu Wang

²,

Rui Zhang

²,

Yihan Diao

²,

Yaoqi Tian

¹ and

Zhengyu Jin

^1,*

¹

State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China

²

School of Life Science and Food Engineering, Huaiyin Institute of Technology, Huai’an 223003, China

^*

Author to whom correspondence should be addressed.

Processes 2020, 8(5), 629; https://doi.org/10.3390/pr8050629

Submission received: 11 April 2020 / Revised: 17 May 2020 / Accepted: 18 May 2020 / Published: 24 May 2020

(This article belongs to the Special Issue Biocatalysis, Enzyme and Process Engineering)

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Abstract

In this study, magnetic Fe₃O₄ nanoparticles coated with polydopamine possessing abundant amino groups (Fe₃O₄@PDA) were conveniently prepared, detailed, and characterized, and then firstly used as a supporting matrix for immobilizing Thermomyces lanuginosus lipase (Fe₃O₄@PDA@TLL). The effects of some crucial factors on the immobilization efficiency were investigated and the optimal protein loading and activity recovery were found to be 156.4 mg/g and 90.9%, respectively. Characterization studies revealed that Fe₃O₄@PDA@TLL displayed a broader pH and temperature adaptability as compared to the free TLL, which allows its use at wider ranges of reaction conditions. With regard to the stabilities, the immobilized TLL clearly displayed improved pH, thermal, and solvent tolerance stabilities compared to the free enzyme, suggesting that the biocompatible Fe₃O₄@PDA might be an outstanding material for immobilizing TLL and acting as alternative support for different enzymes.

Keywords: magnetic nanoparticle; immobilization; Thermomyces lanuginosus lipase; stability

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MDPI and ACS Style

Bi, Y.; Wang, Z.; Zhang, R.; Diao, Y.; Tian, Y.; Jin, Z. Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles. Processes 2020, 8, 629. https://doi.org/10.3390/pr8050629

AMA Style

Bi Y, Wang Z, Zhang R, Diao Y, Tian Y, Jin Z. Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles. Processes. 2020; 8(5):629. https://doi.org/10.3390/pr8050629

Chicago/Turabian Style

Bi, Yanhong, Zhaoyu Wang, Rui Zhang, Yihan Diao, Yaoqi Tian, and Zhengyu Jin. 2020. "Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles" Processes 8, no. 5: 629. https://doi.org/10.3390/pr8050629

APA Style

Bi, Y., Wang, Z., Zhang, R., Diao, Y., Tian, Y., & Jin, Z. (2020). Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles. Processes, 8(5), 629. https://doi.org/10.3390/pr8050629

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Improved Catalytic Properties of Thermomyces lanuginosus Lipase Immobilized onto Newly Fabricated Polydopamine-Functionalized Magnetic Fe₃O₄ Nanoparticles

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