Transglutaminase effects on low temperature gelation of fish protein sols

Myosin polymerization and formation of epsilon-(gamma-glutamyl)lysine linkages were quantified in Alaska pollock surimi gels which contained no additive (control), or a commercial microbial transglutaminase (MTGase). As preincubation ("setting") time at 25 degrees C was increased, the gel...

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Bibliographic Details
Published in:Journal of food science 1997-01, Vol.62 (1), p.20-24
Main Authors: Lee, H.G. (North Carolina State Univ., Raleigh, NC.), Lanier, T.C, Hamann, D.D, Knopp, J.A
Format: Article
Language:English
Subjects:
AMINOACYLTRANSFERASES
ANIMAL PROTEIN
Biological and medical sciences
covalent
crosslink
Enzymes
Fish
Fish and seafood industries
FISH PRODUCTS
FISHES
Food industries
Food science
Fundamental and applied biological sciences. Psychology
linkage
Marine
PECES
POISSON (ANIMAL)
PRODUCTOS DERIVADOS DEL PESCADO
PRODUIT A BASE DE POISSON
PROTEIN CROSSLINKING
PROTEINAS DE ORIGEN ANIMAL
PROTEINE ANIMALE
Proteins
SURIMI
Theragra chalcogramma
TRANSFERASAS
TRANSFERASE
TRANSFERASES
transglutaminase
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Summary:Myosin polymerization and formation of epsilon-(gamma-glutamyl)lysine linkages were quantified in Alaska pollock surimi gels which contained no additive (control), or a commercial microbial transglutaminase (MTGase). As preincubation ("setting") time at 25 degrees C was increased, the gel strength of control and 0.2% MTGase-added samples increased, with greater increases at higher MTGase levels. SDS-PAGE and HPLC analyses showed increasing nondisulfide polymerization and epsilon-(gamma-glutamyl)lysine dipeptide content, with increasing setting time and/or added MTGase. Content of epsilon-(gamma-glutamyl)lysine dipeptide correlated with gel strength (shear stress) and shear modulus at failure (G(f)) for these gels. Higher stresses were measured in samples containing 0.2% MTGase than in controls at corresponding levels of epsilon-(gamma-glutamyl)lysine dipeptide, indicating that rate of myosin polymerization may affect ultimate gel strength
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1997.tb04359.x