Evidence map›Paper›PMID 37819460›Full record

ArticleApplied biochemistry and biotechnology2024

Carboxy-Functionalized Covalent Organic Framework as a Carrier for Lipase Immobilization and Its Application in Inhibitors Screening.

Xue Liu, Jiaqi Wu, Shan Yang, Lingyu Li, Yibing Ji

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Article in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Xue LiuDepartment of Analytical Chemistry, China Pharmaceutical University, 24 TongJiaXiang, Nanjing, 210009, Jiangsu, China.
Jiaqi WuDepartment of Analytical Chemistry, China Pharmaceutical University, 24 TongJiaXiang, Nanjing, 210009, Jiangsu, China.
Shan YangDepartment of Analytical Chemistry, China Pharmaceutical University, 24 TongJiaXiang, Nanjing, 210009, Jiangsu, China.
Lingyu LiDepartment of Analytical Chemistry, China Pharmaceutical University, 24 TongJiaXiang, Nanjing, 210009, Jiangsu, China.
Yibing JiDepartment of Analytical Chemistry, China Pharmaceutical University, 24 TongJiaXiang, Nanjing, 210009, Jiangsu, China. jiyibing@msn.com.ORCID http://orcid.org/0000-0002-8438-4712

Funding

Natural Science Foundation of Jiangsu Province BE2019717
6 · The paper itself

Abstract

Covalent organic frameworks (COFs) with large specific surface areas, high porosity, good stability, and designable structure are promising carriers for immobilized enzymes. It is important to explore lipase inhibitors from natural foods as lipase inhibitors are closely related to the treatment of obesity. In this work, a carboxyl functionalized covalent organic framework (TpBD-3COOH) was prepared by solvothermal method for covalent immobilization of porcine pancreatic lipase (PPL) and obtained the enzyme-decorated COF (PPL@COF). The immobilized lipase showed wider pH and temperature tolerance with the same optimal pH and temperature of 7.5 and 50 ℃ compared to free lipase. After 6 successive reuses, the PPL@COF maintained 53.0% of its original activity. Immobilized lipase also displayed enhanced storage stability (55.4% after 14 days at 4 ℃). When p-nitrophenyl acetate was applied as the substrate, the calculated Michaelis constant was 3.57 mM and the half maximal inhibitory concentration of orlistat was 3.20 μM. Finally, the PPL@COF was used for enzyme inhibitors screening from natural foods combined with UV spectrophotometry, and Hawthorn was screened for excellent lipase inhibitory activity.

Indexed as

Enzyme InhibitorsEnzymes, ImmobilizedLipaseAnimalsEnzyme StabilityHydrogen-Ion ConcentrationKineticsMetal-Organic FrameworksSwineTemperatureEnzyme InhibitorsEnzymes, ImmobilizedLipaseMetal-Organic FrameworksCovalent organic frameworksImmobilized lipaseInhibitors screeningNatural foods

Identifiers

PMID37819460

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.