ArticleAnimal bioscience2026
Evaluation of gel and structural properties of pork myofibrillar protein gels using faba bean protein isolate at various salt concentrations.
Article in Animal bioscience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
objectiveThis study aimed to evaluate the gel and structural properties of pork myofibrillar protein gels (MPGs) using faba bean protein isolate (FBPI) at various salt concentrations.
methodsMPGs were prepared with or without 1 % FBPI under three salt concentrations (0.15, 0.30, and 0.45 M), yielding six treatments. The gel strength, viscosity, and cooking yield were measured. In addition, microstructure, surface hydrophobicity, sulfhydryl group, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis were analyzed to examine the effects of FBPI and salt concentration on the gel and structural properties of MPGs.
resultsMPGs containing 1.0% FBPI had a higher cooking yield, gel strength, protein surface hydrophobicity, and shear stress values than the control groups. The addition of FBPI resulted in more homogenous MPGs with a denser surface compared to the control groups. No interactions in functional properties between FBPI addition and salt concentration were observed, except for gel strength. MPGs at a 0.45 M salt concentration showed a higher cooking yield and hydrophobicity and fewer sulfhydryl groups than those at a 0.15 M salt concentration. The shear stress values at a 0.45 M salt concentration dramatically increased compared to those at 0.15 M and 0.30 M. Furthermore, higher salt concentrations (0.45 M salt) resulted in fewer cavities and a more compact three-dimensional structure.
conclusionHigher salt concentrations may improve the rheological properties of MPGs and influence the effects of FBPI on the viscosity and protein patterns. These findings suggested that controlling salt concentration and FBPI level could be an effective strategy to enhance the gelation and structural characteristics of meat protein systems.
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.