Transglutaminase Effects on Low Temperature Gelation of Fish Protein Sols

Authors

  • H.G. LEE,

    1. Authors Lee, Lanier, and Hamann are with the Dept. of Food Science, North Carolina State Univ., Raleigh, NC 27695-7624, Author Knopp is with the Dept. of Biochemistry, North Carolina State Univ., Raleigh, NC 27695-7624.
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  • T.C. LANIER,

    1. Authors Lee, Lanier, and Hamann are with the Dept. of Food Science, North Carolina State Univ., Raleigh, NC 27695-7624, Author Knopp is with the Dept. of Biochemistry, North Carolina State Univ., Raleigh, NC 27695-7624.
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  • D.D. HAMANN,

    1. Authors Lee, Lanier, and Hamann are with the Dept. of Food Science, North Carolina State Univ., Raleigh, NC 27695-7624, Author Knopp is with the Dept. of Biochemistry, North Carolina State Univ., Raleigh, NC 27695-7624.
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  • J.A. KNOPP

    1. Authors Lee, Lanier, and Hamann are with the Dept. of Food Science, North Carolina State Univ., Raleigh, NC 27695-7624, Author Knopp is with the Dept. of Biochemistry, North Carolina State Univ., Raleigh, NC 27695-7624.
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  • This work was sponsored, in part, by the Univ. of North Carolina Sea Grant College Program by NA-90-AA-D-SG062, Project No. R/SST-15 from the National Oceanic and Atmospheric Administration, NOAA. The U.S. Government is authorized to produce and distribute reprints for governmental purposes notwithstanding any copyright that may appear thereon.

  • Paper No. FS95-53 of the Journal Series of the Dep of Food Science, North Carolina State Univ., Raleigh, NC 27695-7624.

  • Use of trade names in this publication does not imply endorsement by North Carolina Agricultural Research Service, nor criticism of similar ones not mentioned.

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 (Gf) 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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