<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>23(1)</volume><submitter>Wan X</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Aspergillus niger ATCC 20611 is an industrially important fructooligosaccharides (FOS) producer since it produces the β-fructofuranosidase with superior transglycosylation activity, which is responsible for the conversion of sucrose to FOS accompanied by the by-product (glucose) generation. This study aims to consume glucose to enhance the content of FOS by heterologously expressing glucose oxidase and peroxidase in engineered A. niger.&lt;h4>Results&lt;/h4>Glucose oxidase was successfully expressed and co-localized with β-fructofuranosidase in mycelia. These mycelia were applied to synthesis of FOS, which possessed an increased purity of 60.63% from 52.07%. Furthermore, peroxidase was expressed in A. niger and reached 7.70 U/g, which could remove the potential inhibitor of glucose oxidase to facilitate the FOS synthesis. Finally, the glucose oxidase-expressing strain and the peroxidase-expressing strain were jointly used to synthesize FOS, which content achieved 71.00%.&lt;h4>Conclusions&lt;/h4>This strategy allows for obtaining high-content FOS by the multiple enzymes expressed in the industrial fungus, avoiding additional purification processes used in the production of oligosaccharides. This study not only facilitated the high-purity FOS synthesis, but also demonstrated the potential of A. niger ATCC 20611 as an enzyme-producing cell factory.</pubmed_abstract><journal>Microbial cell factories</journal><pagination>76</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10924377</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Effective synthesis of high-content fructooligosaccharides in engineered Aspergillus niger.</pubmed_title><pmcid>PMC10924377</pmcid><pubmed_authors>Zhang J</pubmed_authors><pubmed_authors>Zhang Z</pubmed_authors><pubmed_authors>Wan X</pubmed_authors><pubmed_authors>Sun G</pubmed_authors><pubmed_authors>Liu C</pubmed_authors><pubmed_authors>Zhong Y</pubmed_authors><pubmed_authors>Chang J</pubmed_authors><pubmed_authors>Li K</pubmed_authors><pubmed_authors>Wang L</pubmed_authors></additional><is_claimable>false</is_claimable><name>Effective synthesis of high-content fructooligosaccharides in engineered Aspergillus niger.</name><description>&lt;h4>Background&lt;/h4>Aspergillus niger ATCC 20611 is an industrially important fructooligosaccharides (FOS) producer since it produces the β-fructofuranosidase with superior transglycosylation activity, which is responsible for the conversion of sucrose to FOS accompanied by the by-product (glucose) generation. This study aims to consume glucose to enhance the content of FOS by heterologously expressing glucose oxidase and peroxidase in engineered A. niger.&lt;h4>Results&lt;/h4>Glucose oxidase was successfully expressed and co-localized with β-fructofuranosidase in mycelia. These mycelia were applied to synthesis of FOS, which possessed an increased purity of 60.63% from 52.07%. Furthermore, peroxidase was expressed in A. niger and reached 7.70 U/g, which could remove the potential inhibitor of glucose oxidase to facilitate the FOS synthesis. Finally, the glucose oxidase-expressing strain and the peroxidase-expressing strain were jointly used to synthesize FOS, which content achieved 71.00%.&lt;h4>Conclusions&lt;/h4>This strategy allows for obtaining high-content FOS by the multiple enzymes expressed in the industrial fungus, avoiding additional purification processes used in the production of oligosaccharides. This study not only facilitated the high-purity FOS synthesis, but also demonstrated the potential of A. niger ATCC 20611 as an enzyme-producing cell factory.</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Mar</publication><modification>2026-06-23T03:18:55.066Z</modification><creation>2025-04-04T12:58:59.39Z</creation></dates><accession>S-EPMC10924377</accession><cross_references><pubmed>38461254</pubmed><doi>10.1186/s12934-024-02353-w</doi></cross_references></HashMap>