Tyrosinase-aided protein cross-linking: Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels

Raija Lantto, Eero Puolanne, Kristiina Kruus, Johanna Buchert, Karin Autio

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    56 Citations (Scopus)

    Abstract

    The effects of Trichoderma reesei tyrosinase-catalyzed cross-linking of isolated chicken breast myofibril proteins as a simplified model system were studied with special emphasis on the thermal stability and gel formation of myofibrillar proteins. In addition, tyrosinase-catalyzed cross-linking was utilized to modify the firmness, water-holding capacity (WHC), and microstructure of cooked chicken breast meat homogenate gels.
    According to SDS-PAGE, the myosin heavy chain (MHC) and troponin T were the most sensitive proteins to the action of tyrosinase, whereas actin was not affected to the same extent.
    Calorimetric enthalpy (ΔH) of the major thermal transition associated with myosin denaturation was reduced and with actin denaturation increased in the presence of tyrosinase. Low-amplitude viscoelastic measurements at constant temperatures of 25 °C and 40 °C showed that tyrosinase substantially increased the storage modulus (G‘) of the 4% myofibrillar protein suspension in the 0.35 M NaCl concentration.
    The effect was the most pronounced with high-enzyme dosages and at 40 °C. Without tyrosinase, the G‘ increase was low. Tyrosinase increased the firmness of the cooked phosphate-free and low-meat chicken breast meat homogenate gels compared to the corresponding controls.
    Tyrosinase maintained gel firmness at the control level of the low-salt homogenate gel and weakened it when both salt and phosphate levels were low.
    Tyrosinase improved the WHC of the low-meat and low-salt homogenate gels and maintained it at the level of the corresponding controls of phosphate-free and low-salt/low-phosphate homogenate gels.
    Microstructural characterization showed that a collagen network was formed in the presence of tyrosinase.
    Original languageEnglish
    Pages (from-to)1248-1255
    JournalJournal of Agricultural and Food Chemistry
    Volume55
    Issue number4
    DOIs
    Publication statusPublished - 2007
    MoE publication typeA1 Journal article-refereed

    Keywords

    • Chicken myofibrillar proteins
    • protein modification
    • cross-linking
    • tyrosinase
    • gelation
    • thermal stability
    • texture
    • water-holding capacity
    • microstructure

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