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Transglutaminase Effects on Low Temperature Gelation of Fish Protein Sols
Author(s) -
LEE H.G.,
LANIER T.C.,
HAMANN D.D.,
KNOPP J.A.
Publication year - 1997
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1997.tb04359.x
Subject(s) - lysine , chemistry , dipeptide , myosin , polymerization , tissue transglutaminase , rheology , chromatography , food science , peptide , biochemistry , enzyme , polymer , amino acid , organic chemistry , materials science , composite material
Myosin polymerization and formation of ɛ‐(γ‐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°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 ɛ‐(γ‐glutamyl)lysine dipeptide content, with increasing setting time and/or added MTGase. Content of ɛ‐(γ‐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 ɛ‐(γ‐glutamyl)lysine dipeptide, indicating that rate of myosin polymerization may affect ultimate gel strength.