Discover Community Create You

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

Article

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.

The FEBS journal - 1 Jun 2017

Rico-Díaz Agustín, Ramírez-Escudero Mercedes, Vizoso-Vázquez Ángel, Cerdán M Esperanza, Becerra Manuel, Sanz-Aparicio Julia

Abstract excerpt

β-Galactosidases are biotechnologically interesting enzymes that catalyze the hydrolysis or transgalactosylation of β-galactosides. Among them, the Aspergillus niger β-galactosidase (AnβGal) belongs to the glycoside hydrolase family 35 (GH35) and is widely used in the industry due to its high hydrolytic activity which is used to degrade lactose. We present here its three-dimensional structure in complex with...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspergillus niger
Share to beta-Galactosidase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Glycosides

Share to Hydrolysis

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Substrate Specificity

Source

Identifiers

PMID: 28391618
DOI: 10.1111/febs.14083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.PMID 28391618Read ↗

Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases.Semantic proximity Read ↗

Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3-1,4-Glucans through Distinct Mechanisms.Semantic proximity Read ↗

Glucansucrase Gtf180-ΔN of Lactobacillus reuteri 180: enzyme and reaction engineering for improved glycosylation of non-carbohydrate molecules.Semantic proximity Read ↗

Structural Analysis of β-Fructofuranosidase from Xanthophyllomyces dendrorhous Reveals Unique Features and the Crucial Role of N-Glycosylation in Oligomerization and Activity.Semantic proximity Read ↗

Residue Leu940 has a crucial role in the linkage and reaction specificity of the glucansucrase GTF180 of the probiotic bacterium Lactobacillus reuteri 180.Semantic proximity Read ↗

The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans.Semantic proximity Read ↗

Semirational Engineering of α-Galactosidase for Improvement of Its Thermostability and Transglycosylation Ability.Semantic proximity Read ↗

Modulation of the Activity and Regioselectivity of a Glycosidase: Development of a Convenient Tool for the Synthesis of Specific Disaccharides.Semantic proximity Read ↗

Structures of a glucose-tolerant β-glucosidase provide insights into its mechanism.Semantic proximity Read ↗

Crystal structure of β-glucosidase 1A from Thermotoga neapolitana and comparison of active site mutants for hydrolysis of flavonoid glucosides.Semantic proximity Read ↗

Active site and laminarin binding in glycoside hydrolase family 55.Semantic proximity Read ↗

Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation.Semantic proximity Read ↗

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