Effect of endogenous transglutaminase on threadfin bream surimi gelation

J. Yongsawatdigul, A. Worratao, J. W. Park

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)


Transglutaminase (TGase) activity of threadfin bream mince was 99.6 units/g of dry weight. After washing and screw-pressed dewatering, 44% residual activity was retained. Covalent cross-linking of myosin heavy chain (MHC) was observed at both 25 and 40°C and supported by increased gel strength. When pre-incubation at 40 °C was prolonged to 4 h, breaking force and MHC decreased due to endogenous proteinase(s). TGase activity towards MHC and synthetic substrates was effectively inhibited by iodoacetic acid (IAA). Autolytic activity and degradation of MHC was inhibited by phenylmethanesulfonyl fluoride (PMSF). Addition of 0.2% Ca2+ significantly improved breaking force and increased MHC cross-linking of surimi gels pre-incubated at 40 °C for 2 h.

Original languageEnglish
Pages (from-to)3258-3263
Number of pages6
JournalJournal of Food Science
Issue number9
Publication statusPublished - 2002


  • Cross-linking
  • Myosin heavy chain
  • Threadfin bream
  • Transglutaminase

ASJC Scopus subject areas

  • Food Science


Dive into the research topics of 'Effect of endogenous transglutaminase on threadfin bream surimi gelation'. Together they form a unique fingerprint.

Cite this