51A-42

M. L. DONDERO¹, V. A. Figueroa¹, and E. C. Curotto². (1) Escuela de Alimentos, Universidad Catolica de Valparaiso, Waddington 716, Valparaiso, Chile, (2) Instituto de Quimica, Universidad Catolica de Valparaiso, Brasil 2950, Valparaiso, Chile

JUSTIFICATION. e-(g-glutamyl)lysine is a catalytic product of Transglutaminase (TG) formed between the g-carboxyamide group of glutamine residues and e- amino group of lysine. Surimi gel strength may be enhanced by the addition of microbial transglutaminase (MTGase).

OBJECTIVES. The objective of this work was to evaluate effects of MTGase on texture of surimi from Chilean Jack mackerel (Trachurus murphyi).

METHODS. The qualities of surimi gels were assessed by measuring their breaking force, deformation and gel strength. SDS-PAGE electrophoresis and e-(g-glutamyl)lysine bonds by HPLC were also carried out in the gels.

RESULTS. The addition of MTGase increased gel strength. The optimal attributes were observed at 25ºC by 2 hours, obtaining an increase in breaking force, deformation and gel strength of 218.9, 46.2 and 363.5%, respectively. With the addition of 0.1-0.5% MTGase, gel strength increased significatively. SDS-PAGE revealed that the content of myosin heavy chain (MHC) decreased with increasing setting time and addition of MTGase. The production of e-(g-glutamyl)lysine bonds also increased as a function of setting time and MTGase concentration.

SIGNIFICANCE. Microbial TGase could be employed to improve low mechanical properties of surimi increasing their utilization in minced based-products.