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

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

Applied microbiology and biotechnology - 1 Aug 2014

Ohta Yukari, Hatada Yuji, Hidaka Yuko, Shimane Yasuhiro, Usui Keiko, Ito Tetsuya, Fujita Koki, Yokoi Gaku, Mori Marina, Sato Shona, Miyazaki Takatsugu, Nishikawa Atsushi, Tonozuka Takashi

Abstract excerpt

A β-fructofuranosidase from Microbacterium saccharophilum K-1 (formerly known as Arthrobacter sp. K-1) is useful for producing the sweetener lactosucrose (4(G)-β-D-galactosylsucrose). Thermostability of the β-fructofuranosidase was enhanced by random mutagenesis and saturation mutagenesis. Clones with enhanced thermostability included mutations at residues Thr47, Ser200, Phe447, Phe470, and Pro500. In the highest...

Read the complete abstract on PubMed

Topics

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

Share to Actinomycetales
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to beta-Fructofuranosidase

Share to Enzyme Stability

Share to Hot Temperature

Share to Kinetics

Share to Models, Molecular

Share to Protein Engineering

Source

Identifiers

PMID: 24633372
DOI: 10.1007/s00253-014-5645-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enhancing thermostability and the structural characterization of Microbacterium saccharophilum K-1 β-fructofuranosidase.PMID 24633372Read ↗

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

Semi-rational design in simultaneous improvement of thermostability and activity of β-1,3-glucanase from Alkalihalobacillus clausii KSMK16.Semantic proximity Read ↗

Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution.Semantic proximity Read ↗

Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.Semantic proximity Read ↗

Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability.Semantic proximity Read ↗

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

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01.Semantic proximity Read ↗

Improvement of thermostability and halostability of β-1,3-1,4-glucanase by substituting hydrophobic residue for Lys48.Semantic proximity Read ↗

Balancing α6/α6 barrel kinetic stability and loop flexibility in a thermophilic cellobiose 2-epimerase enhanced lower temperature lactulose biosynthesis.Semantic proximity Read ↗

Additional salt bridges improve the thermostability of 1,4-α-glucan branching enzyme.Semantic proximity Read ↗

Characterization of Sulfolobus solfataricus β-galactosidase mutant F441Y expressed in Pichia pastoris.Semantic proximity Read ↗

Probing the Role of Two Critical Residues in Inulin Fructotransferase (DFA III-Producing) Thermostability from Arthrobacter sp. 161MFSha2.1.Semantic proximity Read ↗

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