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

A natural variant of Bacillus licheniformis alpha-amylase isolated from flour mill wastewaters sheds light on the origin of high thermostability.

Journal of applied microbiology - 1 Jan 2005

Shahhoseini M, Ziaee A-A, Pourbabai A-A, Ghaemi N, Declerck N

Abstract excerpt

AIMS: Understanding the origin of high thermostability exhibited by the alpha-amylase produced by a natural strain of Bacillus licheniformis. METHODS AND RESULTS: The MSH320 alpha-amylase gene has been cloned from a native strain of B. licheniformis isolated from flour mill wastewaters in Kashan, central Iran, and its nucleotide sequence was determined (GenBank Accession Number AF438149). Whereas previously...

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 Bacillus

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

Share to Base Sequence

Share to Hot Temperature

Share to Industrial Waste

Share to Industry

Share to Sequence Alignment

Source

Identifiers

PMID: 15610414
DOI: 10.1111/j.1365-2672.2004.02407.x

Genes

IMPACT

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

A natural variant of Bacillus licheniformis alpha-amylase isolated from flour mill wastewaters sheds light on the origin of high thermostability.PMID 15610414Read ↗

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

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

Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis alpha-amylases and insights into engineering alpha-amylase variants active under acidic conditions.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 ↗

Kinetic characterization of extracellular alpha-amylase from a derepressed mutant of Bacillus licheniformis.Semantic proximity Read ↗

Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution.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 ↗

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

A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.Semantic proximity Read ↗

Enhancing the soluble expression of an amylase in Escherichia coli by the mutations related to its domain interactions.Semantic proximity Read ↗

Alpha-amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity.Semantic proximity Read ↗

A thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes.Semantic proximity Read ↗

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