Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase

• Published in: Food research international Vol. 38; no. 10; pp. 1143 - 1149
• Main Authors: Ramírez-Suárez, J.C., Addo, K., Xiong, Y.L.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01-12-2005; Elsevier
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; breast muscle; Cereal and baking product industries; chicken meat; comminuted muscle food; elasticity (mechanics); Food industries; Fundamental and applied biological sciences. Psychology; gelatinization; Gelation; gels; Gluten; heat treatment; microbial proteins; mixing; muscle protein; Myofibrillar protein; protein-glutamine gamma-glutamyltransferase; restructured muscle food; sarcomeres; storage modulus; thermal properties; Transglutaminase; Triticum aestivum; wheat gluten; wheat protein; Myofibrillar protein; Transglutaminase; Gluten; Gelation; Plant protein; Cereal; Wheat
• ISSN: 0963-9969; 1873-7145
• DOI: 10.1016/j.foodres.2005.04.004

Gluten (Glu) and an acid-extracted protein fraction (AF) from wheat flour were mixed (1:1 ratio) with myofibrillar protein (MP) and treated with microbial transglutaminase (MTGase) to observe the effect on heat-induced gelation. Dynamic rheological properties and thermal denaturation patterns of treated samples were measured, respectively, with an oscillatory rheometer and a differential scanning calorimeter. The storage modulus (
G′) of control MP sample (no MTGase), with a value of 533
Pa at end of heating (77
°C), was not affected (
P
>
0.05) by Glu nor by AF. However, mixed protein samples after the MTGase treatment produced higher gel elasticity values that differed (
P
<
0.05) between samples (1355, 1700 and 1875
Pa at 77
°C for MP, MP/AF, and MP/Glu, respectively). The MP sample underwent three endothermic transitions (peaking at 61.5, 68.0, and 78.5
°C) during thermal scan. The treatment with MTGase and/or addition of Glu or AF tended to lower the temperature for the first transition but raised the temperature for the third transition, suggesting possible interactions of the muscle with non-muscle proteins.