Evidence map›Paper›PMID 27209523›Full record

ArticleExtremophiles : life under extreme conditions2016

Cloning, expression and characterization of a novel cold-active and organic solvent-tolerant esterase from Monascus ruber M7.

Hailun Guo, Yan Zhang, Yanchun Shao, Wanping Chen, Fusheng Chen, Mu Li

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Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 29 citations in OpenAlex.

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  6. Expression and characterization of a 9-cis-epoxycarotenoid dioxygenase fromBiotechnology reports (Amsterdam, Netherlands) · 2018
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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

6 authors at 1 institution in 1 country.

Hailun GuoKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China.
Yan ZhangKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China.
Yanchun ShaoKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China.
Wanping ChenKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China.
Fusheng ChenKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China.
Mu LiKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Ministry of Education, Wuhan, 430070, Hubei, People's Republic of China. limu@mail.hzau.edu.cn.
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cold active esterases are a class of important biocatalysts that exhibit high activity at low temperatures. In this study, a search for putative cold-active esterase encoding genes from Monascus ruber M7 was performed. A cold-active esterase, named Lip10, was isolated, cloned, purified, and characterized. Amino acid sequence analysis reveals that Lip10 contained a conserved sequence motif Gly(173)-Xaa-Ser(175)-Xaa-Gly(177) that is also present in the majority of esterases and lipases. Phylogenetic analysis indicated that Lip10 was a novel microbial esterase. The lip10 gene was cloned and heterologously expressed in Escherichia coli BL21(DE3), resulting in the expression of an active and soluble protein that constituted 40 % of the total cell protein content. Lip10 maintained almost 50 % of its maximal activity at 4-10 °C, with optimal activity at 40 °C. Furthermore, Lip10 retained 184-216 % of its original activity, after incubation in 50 % (v/v) hydrophobic organic solvents for 24 h. The enzyme also exhibited high activity under alkaline conditions and good tolerance to metal ions in the reaction mixture. These results indicate that Lip10 may have potential uses in chemical synthesis and food processing industrial applications as an esterase.

Indexed as

Amino Acid MotifsBenzoatesCold TemperatureDimethyl SulfoxideEnzyme StabilityEsterasesFungal ProteinsMonascusBenzoatesDimethyl SulfoxideEsterasesFungal ProteinsCold activeEsteraseGene cloning and expressionIndustrial applicationsMonascus ruber

Identifiers

PMID27209523
OpenAlexW2398260406

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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.