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

Kinetic characterization of extracellular alpha-amylase from a derepressed mutant of Bacillus licheniformis.

Applied biochemistry and biotechnology - 1 Jan 2000

Ul-Haq Ikram, Ashraf Hamad, Ali Sikander, Qadeer M A

Abstract excerpt

Three strains of Bacillus licheniformis were isolated and screened for alpha-amylase production by solid-state fermentation. Of these, IS-2 gave relatively higher enzyme production (32+/-2.3 U/[g.min]) and was selected for improvement after treatment with N-methylnN-nitro N-nitroso guanidine (NG) or nitrous acid (NA) to enhance its hydrolytic potential. Among the mutant variants, NA-14 gave higher enzyme...

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
Share to Biomass

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

Share to Biotechnology

Share to Carbon

Share to Dietary Fiber

Share to Fermentation

Share to Hot Temperature

Source

Identifiers

PMID: 18035646
DOI: 10.1007/BF02729066

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

Kinetic characterization of extracellular alpha-amylase from a derepressed mutant of Bacillus licheniformis.PMID 18035646Read ↗

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 ↗

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

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

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

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

Amylase hyperproduction by deregulated mutants of the thermophilic fungus Thermomyces lanuginosus.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 ↗

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 ↗

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

Kinetics of improved production and thermostability of an intracellular beta-glucosidase from a mutant-derivative of Cellulomonas biazotea.Semantic proximity Read ↗

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

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