Evidence map›Paper›PMID 39578782›Full record

ArticleBMC biotechnology2024

Enhanced extracellular production of Coprinopsis cinerea laccase Lcc9 in Aspergillus niger by gene expression cassette and bioprocess optimization.

Dongbang Yao, Xiaozhuang Liu, Hui Wang, Juanjuan Liu, Zemin Fang, Yazhong Xiao

Abstract read
In one paragraph

Article in BMC 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

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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.

Dongbang YaoSchool of Life Sciences, Anhui University, Hefei, 230601, China.
Xiaozhuang LiuSchool of Life Sciences, Anhui University, Hefei, 230601, China.
Hui WangSchool of Life Sciences, Anhui University, Hefei, 230601, China.
Juanjuan LiuSchool of Life Sciences, Anhui University, Hefei, 230601, China.
Zemin FangSchool of Life Sciences, Anhui University, Hefei, 230601, China. zemin_fang@ahu.edu.cn.
Yazhong XiaoSchool of Life Sciences, Anhui University, Hefei, 230601, China. yzxiao@ahu.edu.cn.

Funding

Doctoral Research Start-up Funding of Anhui University S020318003/006Joint Funds of the National Natural Science Foundation of China U22A20442Key Projects for Scientific Research Projects of Higher Education Institutions in Anhui Province 2023AH050097National Key Research and Development Program of China 2021YFC2103000
6 · The paper itself

Abstract

backgroundThe laccase Lcc9 from Coprinopsis cinerea has optimal catalytic activity at moderate to alkaline pH conditions, making it invaluable for industrial applications. However, C. cinerea naturally secretes Lcc9 at low expression levels, which limits the industrial application of Lcc9 on a large scale. Recombinant production of Lcc9 using Aspergillus niger would be an effective way to achieve its high production.

resultsThis study achieved the secretory production of Lcc9 in A. niger and established an efficient transformation procedure for A. niger by optimizing its protoplast preparation system. The transformation efficiency of A. niger was increased 3.8-fold under the optimal system (cell wall digestion enzyme solution: 2% cellulase, 1% snailase, 1% lyticase, and 0.5% lysozyme; incubation time: 3 h; incubation temperature: 37 ℃; culture time: 48 h). The extracellular yield of Lcc9 was enhanced by optimizing gene expression cassette and bioprocess. First, the strain AnGgcL (containing P

conclusionsTo our knowledge, this study is the first to report the recombinant extracellular production of the C. cinerea laccase Lcc9 in A. niger and to use SP

Indexed as

Aspergillus nigerLaccaseFermentationFungal ProteinsGene ExpressionProtoplastsRecombinant ProteinsFungal ProteinsLaccaseRecombinant ProteinsAspergillus nigerBioprocessIntegration lociLaccasePromoterSignal peptide

Identifiers

PMID39578782
PMCPMC11583645

What Socratic holds

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LicenceCC BY-NC-ND
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Registered trials

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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 Socratic graph.