Improving the hydrophilic microenvironment surrounding the catalytic site of fructosyltransferase enhances its catalytic ability.

Fanzhi Wang, Suren Singh, Kugen Permaul

Abstract read

In one paragraph

Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

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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

1 citing paper in PubMed.

rDNA-mediated multicopy integration and gene dosage quantification system for microbial zeaxanthin biosynthesis.World journal of microbiology & biotechnology · 2026
Article

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

3 authors.

Fanzhi WangDepartment of Biotechnology and Food Science, Durban University of Technology, Durban, 4001, South Africa.

Suren SinghDepartment of Biotechnology and Food Science, Durban University of Technology, Durban, 4001, South Africa.

Kugen PermaulDepartment of Biotechnology and Food Science, Durban University of Technology, Durban, 4001, South Africa. kugen@dut.ac.za.ORCID http://orcid.org/0000-0001-5032-3092

Funding

National Research Foundation 116019

6 · The paper itself

Abstract

The hydrophilic microenvironment surrounding an enzyme's active site can influence its catalytic activity. This study examines the effect of enhancing this environment in the Aspergillus niger fructosyltransferase, SucC. Bioinformatics analysis identified a cysteine residue (C66) near the catalytic triad (D64, D194, E271) as vital for maintaining the active site's structure and facilitating substrate transport. Simulated mutagenesis suggested that mutating cysteine to serine (C66S) could increase hydrophilicity without altering the structure significantly. This mutation was predicted to enhance substrate affinity, with binding energy changing from -3.65 to -4.14 kcal mol

Indexed as

Aspergillus nigerFungal ProteinsHexosyltransferasesBacterial ProteinsCatalytic DomainHydrophobic and Hydrophilic InteractionsMutagenesis, Site-DirectedOligosaccharidesSaccharomycetalesBacterial ProteinsfructooligosaccharideFungal ProteinsHexosyltransferasesinulosucraseOligosaccharidesCatalytic abilityFructooligosaccharidesFructosyltransferaseHydrophilic microenvironment

Identifiers

PMID40011254

DOI10.1007/s10529-025-03566-8

PMCPMC11865173

What OpenQuestion holds

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LicenceCC BY

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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.