Evidence map›Paper›PMID 27633501›Full record

ArticleScientific reports2016

A highly efficient sorbitol dehydrogenase from Gluconobacter oxydans G624 and improvement of its stability through immobilization.

Tae-Su Kim, Sanjay K S Patel, Chandrabose Selvaraj, Woo-Suk Jung, Cheol-Ho Pan, Yun Chan Kang, Jung-Kul Lee

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 56 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

7 authors at 2 institutions in 1 country.

Tae-Su KimDepartment of Chemical Engineering, Konkuk University, Seoul 05029, Korea.
Sanjay K S PatelDepartment of Chemical Engineering, Konkuk University, Seoul 05029, Korea.
Chandrabose SelvarajDepartment of Chemical Engineering, Konkuk University, Seoul 05029, Korea.
Woo-Suk JungSystems Biotechnology Research Center, KIST Gangneung Institute of Natural Products, 25451, Republic of Korea.
Cheol-Ho PanSystems Biotechnology Research Center, KIST Gangneung Institute of Natural Products, 25451, Republic of Korea.
Yun Chan KangDepartment of Materials Science and Engineering, Korea University, Seoul 02841, Republic of Korea.
Jung-Kul LeeDepartment of Chemical Engineering, Konkuk University, Seoul 05029, Korea.
Konkuk University · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL. The complete 1455-bp codon-optimized gene was amplified, expressed, and thoroughly characterized for the first time. GoSLDH exhibited Km and kcat values of 38.9 mM and 3820 s(-1) toward L-sorbitol, respectively. The enzyme exhibited high preference for NADP(+) (vs. only 2.5% relative activity with NAD(+)). GoSLDH sequencing, structure analyses, and biochemical studies, suggested that it belongs to the NADP(+)-dependent polyol-specific long-chain sorbitol dehydrogenase family. GoSLDH is the first fully characterized SLDH to date, and it is distinguished from other L-sorbose-producing enzymes by its high activity and substrate specificity. Isothermal titration calorimetry showed that the protein binds more strongly to D-sorbitol than other L-sorbose-producing enzymes, and substrate docking analysis confirmed a higher turnover rate. The high oxidation potential of GoSLDH for D-sorbitol was confirmed by cyclovoltametric analysis. Further, stability of GoSLDH significantly improved (up to 13.6-fold) after cross-linking of immobilized enzyme on silica nanoparticles and retained 62.8% residual activity after 10 cycles of reuse. Therefore, immobilized GoSLDH may be useful for L-sorbose production from D-sorbitol.

Indexed as

CalorimetryElectrochemical TechniquesEnzymes, ImmobilizedEnzyme StabilityGluconobacter oxydansIonsKineticsL-Iditol 2-DehydrogenaseMetalsMolecular Docking SimulationNADPRecombinant ProteinsSorbitolSorboseSubstrate SpecificityThermodynamicsEnzymes, ImmobilizedIonsL-Iditol 2-DehydrogenaseMetalsNADPRecombinant ProteinsSorbitolSorbose

Identifiers

PMID27633501
PMCPMC5025769
OpenAlexW2519428661

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.