Species-specificity of suwari [gelation at room temperature] gel-formability of fish flesh paste in which transglutaminase was inactivated

• Published in: Fisheries science Vol. 61; no. 1; pp. 107 - 109
• Main Authors: Niwa, E. (Mie Univ., Tsu (Japan). Faculty of Bioresources), Matsuura, Y, Nowsad, A.A, Kanoh, S
• Format: Journal Article
• Language: English
• Published: 1995
• Subjects: ACIDE GLUTAMIQUE; ACIDO GLUTAMICO; ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; COLLOIDE; COLLOIDS; COLOIDES; ENZYME INHIBITORS; ENZYMIC ACTIVITY; ESPECE; ESPECIES; GELIFICACION; GELIFICATION; GLUTAMIC ACID; INHIBIDORES DE ENZIMAS; INHIBITEUR D'ENZYME; JELLIFICATION; MINCED FISH; PESCADO PICADO; POISSON HACHE; RESISTANCE MECANIQUE; RESISTENCIA MECANICA; SORBITOL; SPECIES; STRENGTH; TRANSFERASAS; TRANSFERASE; TRANSFERASES
• ISSN: 0919-9268; 1444-2906
• DOI: 10.2331/fishsci.61.107

Species-specificity of suwari gel-formability was examined on the pastes from various fish fleshes, in which transglutaminase (TGase) was inactivated. The gels were prepared by setting the pastes with and without adding polyol (4% sucrose-4% sorbitol) and N-ethylmaleimide (NEM) at 35 degree C for 1.5 and 3 h, respectively. The breaking force of the gels was high in the order of red barracuda, jack mackerel, hairtail, Spanish mackerel, stone flounder, Alaska pollack, filefish, bottom threadfin bream, salmon, and cod. The TGase activity of the pastes was generally higher for those fish whose gels showed higher breaking force. As setting progressed, cross-linked myosin heavy chain (cross-linked MHC) in the pastes also increased remarkably in those fish whose gels showed a higher breaking force.