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

Probing the role of asparagine mutation in thermostability of Bacillus KR-8104 α-amylase.

International journal of biological macromolecules - 1 May 2012

Rahimzadeh Mahsa, Khajeh Khosro, Mirshahi Manoochehr, Khayatian Mahmood, Schwarzenbacher Robert

Abstract excerpt

Asparagine deamidation is one of the important determinants of protein thermostability. Here, structure based mutagenesis has been done in order to probe the role of Asn residues in thermostability of a Ca independent Bacillus sp. KR-8104 α-amylase (BKA). Residues involved in potential deamidation processes have been selected and replaced using a site directed mutagenesis. Fourteen different variants were tested...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Amylases
Share to Asparagine

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

Share to Bacillus

Share to Enzyme Activation

Share to Enzyme Stability

Share to Mutagenesis, Site-Directed

Share to Mutant Proteins

Share to Temperature

Source

Identifiers

PMID: 22126991
DOI: 10.1016/j.ijbiomac.2011.11.014

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

Probing the role of asparagine mutation in thermostability of Bacillus KR-8104 α-amylase.PMID 22126991Read ↗

Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase.Semantic proximity Read ↗

Site-directed mutagenesis of a thermostable alpha-amylase from Bacillus stearothermophilus: putative role of three conserved residues.Semantic proximity Read ↗

Enhancing thermostabilization of a newly discovered α-amylase from Bacillus cereus GL96 by combining computer-aided directed evolution and site-directed mutagenesis.Semantic proximity Read ↗

Improving thermostability of Bacillus amyloliquefaciens alpha-amylase by multipoint mutations.Semantic proximity Read ↗

Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency.Semantic proximity Read ↗

Comparison of the wild-type alpha-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of bacillus alpha-amylase.Semantic proximity Read ↗

Lys-Arg mutation improved the thermostability of Bacillus cereus neutral protease through increased residue interactions.Semantic proximity Read ↗

Role of two amino acid residues' insertion on thermal stability of thermophilic α-amylase AMY121 from a deep sea bacterium Bacillus sp. SCSIO 15121.Semantic proximity Read ↗

Biochemical insights into the key residue substituents of an L-asparaginase from Thermococcus kodakarensis and their application in acrylamide mitigation.Semantic proximity Read ↗

Improvement of the acid stability of Bacillus licheniformis alpha amylase by error-prone PCR.Semantic proximity Read ↗

Thermostable bacterial L-asparaginase for polyacrylamide inhibition and in silico mutational analysis.Semantic proximity Read ↗

Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations.Semantic proximity Read ↗

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