Evidence map›Paper›PMID 40627110›Full record

ArticleApplied biochemistry and biotechnology2025

Galactose Oxidase and Horseradish Peroxidase Hybrid Nanoflowers for Biosynthesis of 1-Tetralone.

Hui Wang, Ruichen Gao, Wenxia Liu, Jun Xiong, Wen-Yong Lou, Xiaoling Wu

Abstract read
PubMed Publisher
In one paragraph

Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Hui WangLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China.
Ruichen GaoLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China.
Wenxia LiuLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China.
Jun XiongLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China.
Wen-Yong LouLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China.
Xiaoling WuLab of Applied Biocatalysis, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, School of Food Science and Engineering, South China University of Technology, No. 381 Wushan Road, Guangzhou, 510640, Guangdong, China. wuxl18@scut.edu.cn.

Funding

Basic and Applied Basic Research Foundation of Guangdong Province 2022B1515020013National Key Research and Development Program of China 2023YFA0913600National Natural Science Foundation of China 22378146
6 · The paper itself

Abstract

Organic-inorganic hybrid nanoflowers as novel enzyme immobilization scaffolds have garnered increasing attention due to their high specific surface area and facile preparation conditions. Here, multiple enzyme hybrid nanoflower (GO&HRP-hNF) was obtained by using galactose oxidase (GO) and horseradish peroxidase (HRP) as the inner protein components and copper phosphates as the inorganic agents, which catalyzed the oxidation of 1-tetralol into 1-tetralone. The yield of 1-tetralone obtained from GO&HRP-hNF (49.96 ± 2.8%) was 1.4 times higher than that of the free enzyme system (35.75 ± 1.8%). GO&HRP-hNF displayed comparable kinetic parameters with free GO and remarkably enhanced stability under high temperature. Moreover, GO&HRP-hNF retained 80% of its initial activity even after 30 repeated catalytic cycles, demonstrating its satisfactory reusability. This study provides an avenue for the synthesis of 1-tetralone from 1-tetralol by using immobilized multi-enzyme composites in industrial applications.

Indexed as

Enzymes, ImmobilizedGalactose OxidaseNanostructuresNaphtholsHorseradish PeroxidaseKineticsOxidation-ReductionEnzymes, ImmobilizedGalactose OxidaseHorseradish PeroxidaseNaphthols1-TetraloneEnzyme immobilizationGalactose oxidaseHorseradish peroxidaseHybrid nanoflower

Identifiers

PMID40627110

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.