ArticleBMC biotechnology2026
Characterization of novel cellobiose 2-epimerases from Teredinibacter Haidensis and Cellvibrio Japonicus.
Article in BMC biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCellobiose 2-epimerases (CEs) are promising enzymes that catalyze the conversion of lactose to the bioactive disaccharides epilactose and lactulose. Low-temperature (≤8 °C) lactose bioconversion is essential in dairy applications to prevent microbial contamination. Unfortunately, most CEs are not particularly active at these low temperatures. Therefore, this work aims to discover and characterize novel cold-active CEs.
resultsTwo novel mesophilic CEs from Teredinibacter haidensis (ThCE) and Cellvibrio japonicus (CjCE) were characterized, which showed both epi- and isomerization activity additionally at low temperatures. ThCE showed a maximum epimerization activity (595.4 ± 4.4 nkat/mg protein) at pH 7.5 and 35 °C, while CjCE achieved maximum epimerization activity (887.4 ± 3.9 nkat/mg protein) at pH 9.5 and 40 °C. In addition, CjCE maintained an >80% activity across a wide pH (6-9.5) and temperature range (30-45 °C). Both CEs exhibited significant activity and stability at 8 °C. Specifically, ThCE and CjCE retained around 20 and 40% of their epimerization activity at 8 °C and showed half-lives of 96.3 and 72.2 days, respectively. Moreover, CjCE was also found to be capable of catalyzing the isomerization reaction at 8 °C. The isomerization activity of ThCE and CjCE increased ~370-fold (70.8 ± 2.7 nkat/mg protein) and ~230-fold (66.1 ± 0.3 nkat/mg protein), respectively, at lactose concentrations up to 600 mM (35 °C for ThCE and 40 °C for CjCE). This demonstrates how important it is to conduct investigations of CEs for lactose isomerization to lactulose up to the solubility limit of lactose.
conclusionsThis study identified two new CEs that exhibit interesting catalytic properties for possible application in the generation of disaccharides with prebiotic properties from lactose at low temperatures.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.