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

Research output: Contribution to journalArticleScientificpeer-review

47 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

Fingerprint

Monophenol Monooxygenase
Myofibrils
Meats
breast meat
myofibrils
chicken meat
crosslinking
Meat
breasts
Chickens
Breast
Textures
Gels
texture
gels
chickens
Water
Proteins
phosphates
proteins

Keywords

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

Cite this

@article{9ee7beabd91046d8b7a1ce4c227e08b7,
title = "Tyrosinase-aided protein cross-linking: Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels",
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.",
keywords = "Chicken myofibrillar proteins, protein modification, cross-linking, tyrosinase, gelation, thermal stability, texture, water-holding capacity, microstructure",
author = "Raija Lantto and Eero Puolanne and Kristiina Kruus and Johanna Buchert and Karin Autio",
year = "2007",
doi = "10.1021/jf0623485",
language = "English",
volume = "55",
pages = "1248--1255",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "4",

}

Tyrosinase-aided protein cross-linking : Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels. / Lantto, Raija; Puolanne, Eero; Kruus, Kristiina; Buchert, Johanna; Autio, Karin.

In: Journal of Agricultural and Food Chemistry, Vol. 55, No. 4, 2007, p. 1248-1255.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Tyrosinase-aided protein cross-linking

T2 - Effects on gel formation of chicken breast myofibrils and texture and water-holding of chicken breast meat homogenate gels

AU - Lantto, Raija

AU - Puolanne, Eero

AU - Kruus, Kristiina

AU - Buchert, Johanna

AU - Autio, Karin

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

KW - Chicken myofibrillar proteins

KW - protein modification

KW - cross-linking

KW - tyrosinase

KW - gelation

KW - thermal stability

KW - texture

KW - water-holding capacity

KW - microstructure

U2 - 10.1021/jf0623485

DO - 10.1021/jf0623485

M3 - Article

VL - 55

SP - 1248

EP - 1255

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 4

ER -