Evidence map›Paper›PMID 27527131›Full record

ArticleMolecules (Basel, Switzerland)2016

Laccase Gene Family in Cerrena sp. HYB07: Sequences, Heterologous Expression and Transcriptional Analysis.

Jie Yang, Xinqi Xu, Tzi Bun Ng, Juan Lin, Xiuyun Ye

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 28 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Jie YangFujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fuzhou 350116, Fujian, China. T09136@fzu.edu.cn.
Xinqi XuFujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fuzhou 350116, Fujian, China. xuxinqi@fzu.edu.cn.
Tzi Bun NgSchool of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China. b021770@mailserv.cuhk.edu.hk.
Juan LinFujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fuzhou 350116, Fujian, China. ljuan@fzu.edu.cn.
Xiuyun YeFujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fuzhou 350116, Fujian, China. xiuyunye@fzu.edu.cn.
Fuzhou University · CNChinese University of Hong Kong · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases are a class of multi-copper oxidases with industrial potential. In this study, eight laccases (Lac1-8) from Cerrena sp. strain HYB07, a white-rot fungus with high laccase yields, were analyzed. The laccases showed moderate identities to each other as well as with other fungal laccases and were predicted to have high redox potentials except for Lac6. Selected laccase isozymes were heterologously expressed in the yeast Pichia pastoris, and different enzymatic properties were observed. Transcription of the eight laccase genes was differentially regulated during submerged and solid state fermentation, as shown by quantitative real-time polymerase chain reaction and validated reference genes. During 6-day submerged fermentation, Lac7 and 2 were successively the predominantly expressed laccase gene, accounting for over 95% of all laccase transcripts. Interestingly, accompanying Lac7 downregulation, Lac2 transcription was drastically upregulated on days 3 and 5 to 9958-fold of the level on day 1. Consistent with high mRNA abundance, Lac2 and 7, but not other laccases, were identified in the fermentation broth by LC-MS/MS. In solid state fermentation, less dramatic differences in transcript abundance were observed, and Lac3, 7 and 8 were more highly expressed than other laccase genes. Elucidating the properties and expression profiles of the laccase gene family will facilitate understanding, production and commercialization of the fungal strain and its laccases.

Indexed as

Catalytic DomainCloning, MolecularFermentationFungal ProteinsGene Expression Regulation, EnzymologicGene Expression Regulation, FungalLaccaseModels, MolecularMolecular Docking SimulationMultigene FamilyPolyporaceaeSequence Analysis, DNAFungal ProteinsLaccaseCerrena sp.fermentationheterologous expressionlaccaseqPCR

Identifiers

PMID27527131
PMCPMC6273318
OpenAlexW2492358866

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LicenceCC BY
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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 OpenQuestion graph.