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

Starch digestion and adsorption by beta-amylase of Emericella nidulans (Aspergillus nidulans).

The Journal of applied bacteriology - 1 Mar 1992

Chatterjee B, Ghosh A, Das A

Abstract excerpt

A mutant strain of Emericella nidulans MNU 82 was isolated by multistep mutation. The beta-amylase produced by the mutant was able to digest raw starch. It was readily and strongly adsorbed onto raw starch at pH 5.0. The enzyme to starch ratio was 1950 U/g starch. The enzyme showed no correlation between the capacity of raw starch digestion and adsorption of the enzyme.

Read the complete abstract on PubMed

Topics

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

Share to Adsorption
Share to Aspergillus nidulans
Share to Fermentation

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

Share to Hydrogen-Ion Concentration

Share to Hydrolysis

Share to Mutation

Share to Starch

Source

Identifiers

PMID: 1533208
DOI: 10.1111/j.1365-2672.1992.tb01825.x

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 · 8 closest

Starch digestion and adsorption by beta-amylase of Emericella nidulans (Aspergillus nidulans).PMID 1533208Read ↗

Kinetics of enhanced ethanol productivity using raw starch hydrolyzing glucoamylase from Aspergillus niger mutant produced in solid state fermentation.Semantic proximity Read ↗

Improving the Catalytic Efficiency of Aspergillus fumigatus Glucoamylase toward Raw Starch by Engineering Its N-Glycosylation Sites and Saturation Mutation.Semantic proximity Read ↗

Evidence that the glucoamylases and alpha-amylase secreted by Aspergillus niger are proteolytically processed products of a precursor enzyme.Semantic proximity Read ↗

Analysis of the raw starch-binding domain by mutation of a glucoamylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae.Semantic proximity Read ↗

Cell wall α-1,3-glucan prevents α-amylase adsorption onto fungal cell in submerged culture of Aspergillus oryzae.Semantic proximity Read ↗

Physiological characterisation of recombinant Aspergillus nidulans strains with different creA genotypes expressing A. oryzae alpha-amylase.Semantic proximity Read ↗

Two additional carbohydrate-binding sites of beta-amylase from Bacillus cereus var. mycoides are involved in hydrolysis and raw starch-binding.Semantic proximity Read ↗

Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain.Semantic proximity Read ↗

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