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

Differences in denaturation of genetic variants of soy glycinin.

Journal of agricultural and food chemistry - 17 Jul 2002

Lakemond Catriona M M, De Jongh Harmen H J, Gruppen Harry, Voragen Alphons G J

Abstract excerpt

In heat denaturation studies conducted in the past the genetic variants of glycinin have been considered as a homogeneous group of proteins. In this work the validity of this assumption was tested. It was found by calorimetric studies that glycinin denatures heterogeneously at pH 7.6. When the temperature of isothermal treatment is increased from 70 to 82 degrees C the proportion of glycinin remaining native...

Read the complete abstract on PubMed

Topics

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

Share to Calorimetry
Share to Drug Stability
Share to Glycine max

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

Share to Hot Temperature

Share to Hydrogen-Ion Concentration

Share to Protein Denaturation

Share to Soybean Proteins

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Identifiers

PMID: 12105958
DOI: 10.1021/jf0110405

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

Differences in denaturation of genetic variants of soy glycinin.PMID 12105958Read ↗

Protein recovery in soymilk and various soluble fractions as a function of genotype differences, changes during heating, and homogenization.Semantic proximity Read ↗

Protein glycationin vivo: functional and structural effects on yeast enolaseSemantic proximity Read ↗

Effect of genetic variation on the thermal stability of human serum albumin.Semantic proximity Read ↗

The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants.Semantic proximity Read ↗

Improvement of nutritional value and functional properties of soybean glycinin by protein engineering.Semantic proximity Read ↗

Characterization of beta-conglycinin and glycinin soy protein fractions from four selected soybean genotypes.Semantic proximity Read ↗

Molecular analysis and physicochemical properties of electrophoretic variants of wild soybean Glycine soja storage proteins.Semantic proximity Read ↗

Structure-physicochemical function relationships of soybean beta-conglycinin constituent subunits.Semantic proximity Read ↗

Kinetic stability of designed glycosylation mutants of Coprinus cinereus peroxidase.Semantic proximity Read ↗

Purification, thermal stability, and antigenicity of the immunodominant soybean allergen P34 in soy cultivars, ingredients, and products.Semantic proximity Read ↗

Purification, crystallization and preliminary crystallographic analysis of soybean mature glycinin A1bB2.Semantic proximity Read ↗

Rheological properties of concentrated skim milk: influence of heat treatment and genetic variants on the changes in viscosity during storage.Semantic proximity Read ↗

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