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

B-factor-saturation mutagenesis as a strategy to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus.

Journal of biotechnology - 10 Jun 2018

Ge Lin, Li Dongdong, Wu Tao, Zhao Linguo, Ding Gang, Wang Zhenzhong, Xiao Wei

Abstract excerpt

The α-L-Rhamnosidase is an important enzyme with applications in the food and pharmaceutical industries because it can release terminal L-rhamnose residues from various natural products. In this study, the B-factor-saturation mutagenesis strategy was used to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus. The D594Q and G827K/D594Q mutant enzymes were obtained by screening a series of...

Read the complete abstract on PubMed

Topics

Aspergillus
Crystallography, X-Ray
Enzyme Stability
Fungal Proteins
Glycoside Hydrolases
Half-Life

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Hot Temperature

Hydrogen Bonding

Models, Molecular

Mutation

Protein Structure, Tertiary

Quercetin

Source

Identifiers

PMID: 29605638
DOI: 10.1016/j.jbiotec.2018.03.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

B-factor-saturation mutagenesis as a strategy to increase the thermostability of α-L-rhamnosidase from Aspergillus terreus.PMID 29605638Read ↗

Efficiency enhancement in Aspergillus niger α-L-rhamnosidase reverse hydrolysis by using a tunnel site rational design strategy.Semantic proximity Read ↗

A study of targeted mutation of l-rhamnose isomerase to improve the conversion efficiency of D-allose.Semantic proximity Read ↗

Mutagenesis for Improvement of Activity and Stability of Prolyl Aminopeptidase from Aspergillus oryzae.Semantic proximity Read ↗

Improvement of enzymatic properties of Rhizopus oryzae α-amylase by site-saturation mutagenesis of histidine 286.Semantic proximity Read ↗

Enhancing the Thermostability of Serratia plymuthica Sucrose Isomerase Using B-Factor-Directed Mutagenesis.Semantic proximity Read ↗

Reshaping the Activity-Stability Landscape of a 1,2-Rhamnosyltransferase via Distal Mutational Engineering.Semantic proximity Read ↗

Improving enzyme activity of glucosamine-6-phosphate synthase by semi-rational design strategy and computer analysis.Semantic proximity Read ↗

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

Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger.Semantic proximity Read ↗

Thermostability Enhancement of Streptomyces mobaraensis Transglutaminase by Folding Free Energy-Guided Helix-Corner Motif Engineering.Semantic proximity Read ↗

Enhancing thermostability and the structural characterization of Microbacterium saccharophilum K-1 β-fructofuranosidase.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 ↗

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