Evidence map›Paper›PMID 42163425›Full record

ArticleJournal of the science of food and agriculture2026

Rational engineering of ribitol dehydrogenase for enhanced thermostability and efficient biocatalytic production of allitol.

Tianwen Shang, Jiangang Yang, Yan Men, Xuegang Luo, Yueming Zhu, Yuanxia Sun

Abstract read
In one paragraph

Article in Journal of the science of food and agriculture, 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

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

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Tianwen ShangCollege of Biological Engineering, Tianjin University of Science and Technology, Tianjin, China.
Jiangang YangNational Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.ORCID https://orcid.org/0000-0001-9463-8862
Yan MenNational Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.
Xuegang LuoCollege of Biological Engineering, Tianjin University of Science and Technology, Tianjin, China.
Yueming ZhuNational Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.ORCID https://orcid.org/0000-0002-6592-3733
Yuanxia SunNational Engineering Laboratory for Industrial Enzymes, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin, China.

Funding

Key Technology Research and Development Program of Shandong Province 2023CXGC010714National Key R&D Program of China 2021YFA0910604Natural Science Foundation Program of Tianjin Grant Type A 25JCJQJC00130Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project TSBICIP-IJCP-002
6 · The paper itself

Abstract

backgroundAllitol is a rare sugar alcohol with potential as a low-calorie sweetener and food ingredient; however, its biocatalytic production from d-allulose is limited by the thermostability and cofactor efficiency of the ribitol dehydrogenases (RDH).

resultsIn this study, the RDH from Klebsiella oxytoca was engineered for enhanced thermostability using consensus-guided mutagenesis targeting non-conserved, non-active-site residues, followed by stepwise combination. The resulting M4 mutant showed markedly improved thermostability, with its melting temperature (T

conclusionThis study significantly improved the thermostability of RDH using consensus-guided interfacial design and constructed a cofactor-regenerating enzyme complex for the efficient biocatalytic production of allitol. © 2026 Society of Chemical Industry.

Indexed as

Bacterial ProteinsKlebsiella oxytocaRibitolSugar AlcoholsBiocatalysisEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationKineticsMolecular Dynamics SimulationProtein EngineeringSugar Alcohol DehydrogenasesSweetening AgentsBacterial ProteinsRibitolribitol 2-dehydrogenaseSugar Alcohol DehydrogenasesSugar AlcoholsSweetening Agentsallitolcofactor regenerationenzyme complexprotein engineeringribitol dehydrogenasethermostability

Identifiers

PMID42163425
PMCPMC13442759

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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.