ArticleFood chemistry: X2025
NaCl-thermal synergy mediates structural transitions in hsian-tsao polysaccharide-myosin complexes to influence flavor-binding selectivity.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsian-tsao polysaccharide (HTP) with preferable gel-enhancing and bioactive properties improved surimi quality. This study elucidated how NaCl concentration (0.2-1.0 mol/L) and heating protocols (setting: 40 °C/30 min; two-step heating: 40 °C/30 min + 90 °C/20 min) modulated HTP-myosin complexation and its selective binding to off-flavors (1-octen-3-ol, hexanal, heptanal, nonanal). Associative phase separation occurred in HTP-myosin systems, while myosin transitioned from aggregation to dissolution with increasing NaCl concentration. Setting facilitated HTP-myosin complexation via electrostatic-hydrophobic interactions. HTP reduced myosin aggregation (26.24 % reduction in particle size at 0.6 mol/L NaCl) and increased sulfhydryl groups (17.02 % at 0.4 mol/L NaCl). The α-helix-to-β-sheet transitions reduced aldehyde-binding affinity but enhanced 1-octen-3-ol binding. Two-step heating promoted hydrophobic crosslinking, elevating turbidity and reducing flavor binding by 17.44 %-48.75 %. High NaCl (≥0.8 mol/L) induced electrostatic shielding, accelerating flavor release. PCA linked α-helix loss to alcohol release and β-sheet/sulfhydryl content to aldehyde retention, proposing NaCl-thermal strategies for surimi texture-flavor optimization.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.