Evidence map›Paper›PMID 42400745›Full record

ArticleApplied biochemistry and biotechnology2026

Characterization and Immobilization of a High Activity Lysine Decarboxylase from Serratia Proteamaculans NJ303 for Cadaverine Production.

Guoguang Wei, Ning Zhou, Jie Wei, Alei Zhang, Kequan Chen, Hao He

Abstract read
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Article in Applied biochemistry and biotechnology, 2026. 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

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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

6 authors.

Guoguang Wei *Inner Mongolia key laboratory of synthetic biology, Specialized Technology Research and Pilot Public Service Platform for Biological Fermentation in Inner Mongolia, Center for Energy Conservation and Emission Reduction in Fermentation Industry in Inner Mongolia, College of Chemical Engineering, Engineering Research Center of Inner Mongolia for Green Manufacturing in Bio-fermentation Industry, Inner Mongolia University of Technology, Hohhot, Inner Mongolia, 010051, China.
Ning Zhou *Petrochemical Research Institute of Petrochina Co., Ltd, Beijing, 102206, China.
Jie WeiPetrochemical Research Institute of Petrochina Co., Ltd, Beijing, 102206, China.
Alei ZhangState Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Kequan ChenState Key Laboratory of Materials-Oriented Chemical Engineering, College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, 211816, China.
Hao HePetrochemical Research Institute of Petrochina Co., Ltd, Beijing, 102206, China. hehao010@petrochina.com.cn.

Funding

Jiangsu Funding Program for Excellent Postdoctoral Talent 2022ZB390Major Science and Technology Special Project of Petrochina Co., Ltd. 2024ZZ47National Natural Science Foundation of China 22278220, U21B2097Science and Technology Development Project (Refining and Chemicals Business Sector) of Petrochina Co., Ltd. 21-LH-38-05the Inner Mongolia 2024 First-class Discipline Scientific Research Special Project YLXKZX-NGD-048the National Natural Science Foundation for Young Scientists of China 22408167
6 · The paper itself

Abstract

Cadaverine, an essential precursor for bio-based nylon PA5X production, has emerged as a highly valuable compound in the engineered plastics and synthetic fibers industry. Current industrial biomanufacturing of cadaverine depends critically on the enzymatic activity of L-lysine decarboxylase (LDC). In this investigation, we systematically evaluated ten LDC variants originating from six distinct bacterial species, all cloned and expressed in Escherichia coli BL21(DE3). Comprehensive characterization identified SpLDC from Serratia proteamaculans as the most promising candidate, demonstrating exceptional catalytic activity under alkaline conditions. Enzymatic analysis showed that SpLDC established optimal activity at pH 6.5 and 52 °C, with remarkable stability maintained between pH 5.5-8.0 and temperatures of 37-52 °C during prolonged 12-hour incubations. Kinetic studies revealed favorable catalytic parameters (K

Indexed as

Bacterial ProteinsCadaverineCarboxy-LyasesEnzymes, ImmobilizedSerratiaEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationKineticsTemperatureBacterial ProteinsCadaverineCarboxy-LyasesEnzymes, Immobilizedlysine decarboxylaseCadaverineEnzymatic propertiesImmobilizedLysine decarboxylaseRecyclable catalysts

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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.