ArticleBiotechnology for biofuels2020
Hydrophobic pore space constituted in macroporous ZIF-8 for lipase immobilization greatly improving lipase catalytic performance in biodiesel preparation.
Article in Biotechnology for biofuels, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- Enzymatic synthesis of phosphatidyl-EPA/DHA using Candida antarctica lipase B immobilized on mesoporous MIL-88 A.Bioresources and bioprocessing · 2025Article
- Tailored Metal-Organic Framework-Based Enzyme Hybrids: Immobilization Strategies, Improved Performance, and Biological Applications.Small science · 2025Review
- Article
- Anchoring of Polymer Loops on Enzyme-Immobilized Mesoporous ZIF-8 Enhances the Recognition Selectivity of Angiotensin-Converting Enzyme Inhibitory Peptides.Molecules (Basel, Switzerland) · 2023Article
- Immobilization of Lipase fromACS omega · 2022Article
- Magnetic COFs as satisfied support for lipase immobilization and recovery to effectively achieve the production of biodiesel by great maintenance of enzyme activity.Biotechnology for biofuels · 2021Article
- Pristine and Poly(Dimethylsiloxane) Modified Multi-Walled Carbon Nanotubes as Supports for Lipase Immobilization.Materials (Basel, Switzerland) · 2021Article
- Lipase Immobilization on Macroporous ZIF-8 for Enhanced Enzymatic Biodiesel Production.ACS omega · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDuring lipase-mediated biodiesel production, by-product glycerol adsorbing on immobilized lipase is a common trouble that hinders enzymatic catalytic activity in biodiesel production process. In this work, we built a hydrophobic pore space in macroporous ZIF-8 (named as M-ZIF-8) to accommodate lipase so that the generated glycerol would be hard to be adsorbed in such hydrophobic environment. The performance of the immobilized lipase in biodiesel production as well as its characteristics for glycerol adsorption were systematically studied. The PDMS (polydimethylsiloxane) CVD (chemical vapor deposition) method was utilized to get hydrophobic M-ZIF-8-PDMS with hydrophobic macropore space and then ANL (
resultsANL@M-ZIF-8-PDMS presented higher enzymatic activity recovery and better biodiesel production catalytic performance compared to ANL@M-ZIF-8. Further study revealed that less glycerol adsorption was observed through the hydrophobic modification, which may attribute to the improved immobilized lipase performance during biodiesel production and ANL@M-ZIF-8-PDMS remained more than 96% activity after five cycles' reuse. Through secondary structure and kinetic parameters' analysis, we found that ANL@M-ZIF-8-PDMS had lower extent of protein aggregation and twice catalytic efficiency (
conclusionsHydrophobic pore space constituted in macroporous ZIF-8 for lipase immobilization greatly improved lipase catalytic performance in biodiesel preparation. The hydrophobic modification time showed negligible influence on the reusability of the immobilized lipase. This work broadened the prospect of immobilization of enzyme on MOFs with some inspiration.
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