Evidence map›Paper›PMID 42377560›Full record

ArticleArchives of microbiology2026

Improving high-degree-polymerization GOS synthesis of a marine cold-active β-galactosidase via semi-rational design.

Lin Pan, Yali Zhang, Zhe Wang, Chenxu Fan, Qionghui You, Jiahong Wu, Fangqi Feng, Xiaohui Wang

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Article in Archives of microbiology, 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

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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.

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Lin PanCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Yali ZhangCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Zhe WangCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Chenxu FanCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Qionghui YouCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Jiahong WuCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Fangqi FengCollege of Life and Health, Dalian University, Dalian, Liaoning, China.
Xiaohui WangCollege of Life and Health, Dalian University, Dalian, Liaoning, China. wangxiaohui@dlu.edu.cn.

Funding

Dalian Youth Science and Technology Star Project 2017RQ155National Natural Science Foundation of China for Young Scientists Project 31500039Natural Science Foundation of Liaoning Province 20180550728
6 · The paper itself

Abstract

Cold-active β-galactosidase has significant application value in the enzymatic synthesis of galacto-oligosaccharides (GOS); however, its low transglycosylation efficiency and poor selectivity toward high-degree polymerization (DP) products remain major challenges. In this study, a cold-active β-galactosidase (K3-β-gal) from marine Bacillus sp. K-3 was cloned and expressed. Four mutants (R252M, F261W, Y281R, and F355K) were constructed via semi-rational design, among which R252M exhibited markedly enhanced transglycosylation activity. Compared with the wild-type enzyme, R252M showed no change in optimum temperature (20 °C) or optimum pH (6.0), and retained good stability under low-temperature and weakly acidic conditions. The total GOS yield increased from 21.68% to 38.12% (a 75.83% improvement), and the DP4/DP3 ratio increased from 0.95 to 2.6, while the hydrolytic activity (k

Indexed as

BacillusBacterial Proteinsbeta-GalactosidaseOligosaccharidesCold TemperatureEnzyme StabilityGalactoseGlycosylationHydrogen-Ion ConcentrationKineticsMolecular Dynamics SimulationPolymerizationSubstrate SpecificityBacterial Proteinsbeta-GalactosidaseGalactoseOligosaccharidesHigh-DP galacto-oligosaccharidesOld-active β-galactosidaseSemi-rational designTransglycosylation efficiency

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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.