Woody breast meat has recently become prevalent in the broiler industry in both the United States and European Union. Recent publications have described the meat quality characteristics of woody breast meat as having hardened areas and pale ridge-like bulges at both the caudal and cranial regions of the breast. The present study investigated the meat quality (pH, color, cooking loss, and shear force) and protein quality characteristics (protein and salt-soluble protein content) in woody breast meat as compared to normal breast meat. In addition, the differences in the muscle proteome profiles of woody and normal breast meat were characterized. Results indicated that woody breast meat had a greater average pH (P < 0.0001) and cooking loss (P = 0.001) than normal breast meat, but woody breast meat did not differ in shear force (P > 0.05) in comparison to normal breast meat samples. The L*, a*, and b* values of woody breast fillets were greater than normal breast fillets (P < 0.0001 to L*; P = 0.002 to a*; P = 0.016 to b*). The woody breast meat had more fat (P < 0.0001) and moisture (P < 0.021) and less protein (P < 0.0001) and salt-soluble protein (P < 0.0001) when compared with normal breast fillets. Whole muscle proteome analysis indicated 8 proteins that were differentially expressed (P < 0.05) between normal and woody breast meat samples. The differences in muscle proteome between normal and woody breast meat indicated an increased oxidative stress in woody breast meat when compared to normal meat. In addition, the abundance of some glycolytic enzymes, which are critical to the regeneration of adenosine triphosphate (ATP) in postmortem muscles, was lower in woody breast meat than in normal breast meat. Proteomic differences provide additional information on the biochemical pathways and genetic variations that lead to woody breast meat. Further research should be conducted to elucidate the genetic and nutritional contributions to the proliferation of woody breast meat in the United States.
To
understand the umami taste of fermented broad bean
paste (FBBP)
and explore the umami mechanism, eight peptides (PKALSAFK, NKHGSGK,
SADETPR, EIKKAALDANEK, DALAHK, LDDGR, and GHENQR) were separated and
identified via ultrafiltration, RP-HPLC, and UPLC-QTOF-MS/MS methods.
Sensory experiments suggested that eight novel peptides showed umami/umami-enhancing
and salt-enhancing functions. Significantly, the threshold of EIKKAALDANEK
in aqueous solution exceeded that of most umami peptides reported
in the past 5 years. The omission test further confirmed that umami
peptides contributed to the umami taste of FBBP. Molecular docking
results inferred that all peptides easily bind with Ser, Glu, His,
and Asp residues in T1R3 through hydrogen bonds and electrostatic
interactions. The aromatic interaction, hydrogen bond, hydrophilicity,
and solvent-accessible surface (SAS) were the main interaction forces.
This work may contribute to revealing the secret of the umami taste
of FBBP and lay the groundwork for the efficient screening of umami
peptides.
In this study, 100% polyester mesh fabrics were used as ham nets. The nets were treated with 40% propylene glycol (PG), 1% propylene glycol alginate (PGA), and 1% carrageenan. The treated and untreated nets were evaluated to determine any significant changes in terms of mechanical properties. Fabric weight (ASTM D3776), elastic properties (BS EN 14704-1:2005), abrasion resistance (ASTM D4966) and breaking strength (ASTM D5034-09) were tested. The morphology of 100% polyester fiber was also observed by scanning electron microscopy (SEM) images. Surface morphology of both treated and untreated fabric was also observed. No significant changes occurred in the mechanical properties that would affect the dry-cured ham aging process. Treated samples were stronger than untreated samples with respect to abrasion resistance, weight of the fabric in unit area (GSM), and tensile strength. This study indicates that these nets could be used to age dry-cured hams as part of a methyl bromide replacement strategy.
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