Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Topics Community

Article

A novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 mutants.

Journal of the science of food and agriculture - 1 May 2015

Mata-Gómez Marco A, Heerd Doreen, Oyanguren-García Iñigo, Barbero Francis, Rito-Palomares Marco, Fernández-Lahore Marcelo

Abstract excerpt

BACKGROUND: In the food industry, the use of pectinase preparations with high pectin esterase (PE) activity leads to the release of methanol, which is strictly regulated in food products. Herein, a pectin-degrading enzyme (PDE) complex exhibiting low PE activity of three Aspergillus sojae ATCC 20235 mutants (M3, DH56 and Guserbiot 2.230) was investigated. Production of exo-/endo-polygalacturonase (PG),...

Topics

Aspergillus niger
Beta vulgaris
Culture Media
Esterases
Esterification
Fermentation
Humans
Lyases
Methanol
Multienzyme Complexes
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Pectins

Polygalacturonase

Source

Identifiers

PMID: 25103563
DOI: 10.1002/jsfa.6864

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A novel pectin-degrading enzyme complex from Aspergillus sojae ATCC 20235 mutants.PMID 25103563Read ↗

Effect of physicochemical parameters on the polygalacturonase of an Aspergillus sojae mutant using wheat bran, an agro-industrial waste, via solid-state fermentation.Semantic proximity Read ↗

A Novel Acid-Stable Endo-Polygalacturonase from Penicillium oxalicum CZ1028: Purification, Characterization, and Application in the Beverage Industry.Semantic proximity Read ↗

A low-temperature polygalacturonase from P. occitanis: characterization and application in juice clarification.Semantic proximity Read ↗

Multi-omics analysis of a traditional fermented food reveals a byproduct-associated subpopulation of <i>Neurospora intermedia</i> for waste-to-food upcyclingSemantic proximity Read ↗

Differential proteomics reveals main determinants for the improved pectinase activity in UV-mutagenized Aspergillus niger strain.Semantic proximity Read ↗

Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis.Semantic proximity Read ↗

Gamma-polyglutamic acid (gamma-PGA) produced by Bacillus amyloliquefaciens C06 promoting its colonization on fruit surface.Semantic proximity Read ↗

Structure and Properties of a Non-processive, Salt-requiring, and Acidophilic Pectin Methylesterase from Aspergillus niger Provide Insights into the Key Determinants of Processivity Control.Semantic proximity Read ↗

The F-box protein gene exo-1 is a target for reverse engineering enzyme hypersecretion in filamentous fungi.Semantic proximity Read ↗

A comparative secretome analysis of industrial Aspergillus oryzae and its spontaneous mutant ZJGS-LZ-21.Semantic proximity Read ↗

Hyperproduction of β-Glucanase Exg1 Promotes the Bioconversion of Mogrosides in Saccharomyces cerevisiae Mutants Defective in Mannoprotein Deposition.Semantic proximity Read ↗

EcXyl43 β-xylosidase: molecular modeling, activity on natural and artificial substrates, and synergism with endoxylanases for lignocellulose deconstruction.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.