Enzyme-aided modification of chicken-breast myofibril proteins: Effect of laccase and transglutaminase on gelation and thermal stability

Raija Lantto (Corresponding Author), E. Puolanne, Nisse Kalkkinen, Johanna Buchert, Karin Autio

Research output: Contribution to journalArticleScientificpeer-review

67 Citations (Scopus)

Abstract

The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS−PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS−PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3% protein content and a constant temperature of 40 °C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G‘) of 3% protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G‘ increased 32 and 64% at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G‘ of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G‘ below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.
Original languageEnglish
Pages (from-to)9231 - 9237
Number of pages7
JournalJournal of Agricultural and Food Chemistry
Volume53
Issue number23
DOIs
Publication statusPublished - 2005
MoE publication typeA1 Journal article-refereed

Fingerprint

Laccase
Transglutaminases
laccase
Myofibrils
protein-glutamine gamma-glutamyltransferase
myofibrils
Gelation
gelation
thermal stability
breasts
Chickens
Breast
Thermodynamic stability
Hot Temperature
chickens
Enzymes
enzymes
Proteins
proteins
heat stability

Keywords

  • chicken myofibril proteins
  • protein modification
  • cross-linking
  • transglutaminase
  • laccase
  • gelation
  • storage modulus
  • isothermal heating
  • heat stability

Cite this

@article{460930013b584d379df9f3cac3a3959d,
title = "Enzyme-aided modification of chicken-breast myofibril proteins: Effect of laccase and transglutaminase on gelation and thermal stability",
abstract = "The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS−PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS−PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3{\%} protein content and a constant temperature of 40 °C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G‘) of 3{\%} protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G‘ increased 32 and 64{\%} at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G‘ of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G‘ below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.",
keywords = "chicken myofibril proteins, protein modification, cross-linking, transglutaminase, laccase, gelation, storage modulus, isothermal heating, heat stability",
author = "Raija Lantto and E. Puolanne and Nisse Kalkkinen and Johanna Buchert and Karin Autio",
year = "2005",
doi = "10.1021/jf051602a",
language = "English",
volume = "53",
pages = "9231 -- 9237",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society ACS",
number = "23",

}

Enzyme-aided modification of chicken-breast myofibril proteins : Effect of laccase and transglutaminase on gelation and thermal stability. / Lantto, Raija (Corresponding Author); Puolanne, E.; Kalkkinen, Nisse; Buchert, Johanna; Autio, Karin.

In: Journal of Agricultural and Food Chemistry, Vol. 53, No. 23, 2005, p. 9231 - 9237.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Enzyme-aided modification of chicken-breast myofibril proteins

T2 - Effect of laccase and transglutaminase on gelation and thermal stability

AU - Lantto, Raija

AU - Puolanne, E.

AU - Kalkkinen, Nisse

AU - Buchert, Johanna

AU - Autio, Karin

PY - 2005

Y1 - 2005

N2 - The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS−PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS−PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3% protein content and a constant temperature of 40 °C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G‘) of 3% protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G‘ increased 32 and 64% at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G‘ of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G‘ below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.

AB - The effect of laccase and transglutaminase (TG) on cross-linking, gelation, and thermal stability of salt-soluble chicken-breast myofibril proteins was investigated at pH 6. Both enzymes modified the protein pattern detected by SDS−PAGE. Identification of proteins by peptide mass mapping showed that myosin heavy chain (MHC) and troponin T were the most affected proteins. These proteins faded or disappeared as a function of the incubation time with both enzymes on SDS−PAGE. The molecular weight of actin was not, however, affected by either enzyme. The effects that the enzymes had on the gel formation of chicken-breast myofibrils were studied in 0.35 and 0.60 M NaCl solutions at 3% protein content and a constant temperature of 40 °C by using a small deformation viscoelastic measurement. TG substantially increased the storage modulus (G‘) of 3% protein in 0.35 M NaCl. Without the enzymes, gelation was insignificant in 0.35 M NaCl. The increased solubility of the proteins at 0.60 M NaCl intensified gelation with TG. G‘ increased 32 and 64% at dosages of 10 and 100 nkat of TG, respectively. Also, laccase increased G‘ of the gel in 0.60 M salt concentration. However, a high laccase dosage decreased the magnitude of G‘ below the control level. Differential scanning calorimetric (DSC) measurements indicated slightly reduced myosin heat stability after TG pretreatment and increased actin heat stability with both enzymes. Maximum transition temperatures did not alter with either enzyme.

KW - chicken myofibril proteins

KW - protein modification

KW - cross-linking

KW - transglutaminase

KW - laccase

KW - gelation

KW - storage modulus

KW - isothermal heating

KW - heat stability

U2 - 10.1021/jf051602a

DO - 10.1021/jf051602a

M3 - Article

VL - 53

SP - 9231

EP - 9237

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 23

ER -