Transglutaminase Effects on Low Temperature Gelation of Fish Protein Sols

ABSTRACT 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...

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Bibliographic Details
Published in:Journal of Food Science
Main Authors: LEE, H.G., LANIER, T.C., HAMANN, D.D., KNOPP, J.A.
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 1997
Subjects:
alaska pollock
Alaska
Online Access:http://dx.doi.org/10.1111/j.1365-2621.1997.tb04359.x
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2621.1997.tb04359.x
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2621.1997.tb04359.x/fullpdf
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Summary:ABSTRACT 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.

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