Transglutaminase Effects on Low Temperature Gelation of Fish Protein Sols |
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| Authors: | HG LEE TC LANIER DD HAMANN JA KNOPP |
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| Affiliation: | 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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| Abstract: | Myosin polymerization and formation of ?-(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 ?-(γ-glutamyl)lysine dipeptide content, with increasing setting time and/or added MTGase. Content of ?-(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 ?-(γ-glutamyl)lysine dipeptide, indicating that rate of myosin polymerization may affect ultimate gel strength. |
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| Keywords: | transglutaminase surimi covalent linkage crosslink |
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