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Record W4414722527 · doi:10.1016/j.foodhyd.2025.112066

Structure-function characterization and gelation mechanisms of mung bean albumin and globulin fractions

2025· article· en· W4414722527 on OpenAlexafffund
Cindy Lalagüe, Ugo Berthelot, G. J. Brisson, Alain Doyen

Bibliographic record

VenueFood Hydrocolloids · 2025
Typearticle
Languageen
FieldAgricultural and Biological Sciences
TopicProteins in Food Systems
Canadian institutionsUniversité Laval
FundersMitacsWyoming Humanities
KeywordsIsoelectric pointAlbuminGlobulinSolubilityFraction (chemistry)Beta globulins

Abstract

fetched live from OpenAlex

This study aimed to evaluate the surface properties, secondary structures, solubilities, and gelling behaviors of purified mung bean globulins and albumins. The globulin fraction (88.44% protein purity) was isolated by isoelectric precipitation from a mung bean protein isolate produced by ultrafiltration-diafiltration (UF-DF), while the albumin fraction (80.72% protein purity) was purified from the soluble fraction using UF-DF. The albumin fraction maintained consistent solubility (∼50%) from pH 2.0 to pH 8.0, whereas the globulin fraction exhibited a U-shaped solubility curve, with a marked decrease near its isoelectric point and maximum solubility at pH 8.0 (91.44%). Albumins exhibited smaller particle sizes compared to globulins and were characterized by a significantly lower concentration of free sulfhydryl groups (5.79 vs 9.77 μmol/mL). The albumin fraction had a lower minimum gelation concentration (4%) compared to the globulin fraction (8%), yet albumin gels formed weaker networks, with lower water retention (73.65%) compared to globulin gels (93.59%) at 8% proteins. Rheological and microscopic analyses supported these findings, revealing a higher elastic modulus (G′) for globulin gels (8.91 Pa vs 1.08 Pa) and a denser microstructure, indicating stronger protein incorporation and more extensive intermolecular bonding. Globulin gels were formed primarily through hydrophobic interactions with no involvement of electrostatic or disulfide bonds. In contrast, albumin gels were formed mainly through electrostatic interactions, followed by hydrophobic interactions, and characterized by a high proportion of unbound proteins (25.5%). Based on these results, mechanisms were proposed to illustrate the interactions and proteins involved in the formation of albumin and globulin gels. • Mung bean albumins and globulins are efficiently separated by pH precipitation. • Albumins and globulins differ in structural and physicochemical properties. • Albumins form coarse particulate gels linked by electrostatic interactions. • Globulins form fine particulate gel linked by hydrophobic interactions. • Globulin gels show higher firmness and water retention than albumin gels.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: none
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.606
Threshold uncertainty score0.212

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.008
GPT teacher head0.202
Teacher spread0.194 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations5
Published2025
Admission routes2
Has abstractyes

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