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Título

Study of two different cold restructuring processes using two different qualities of hake (Merluccius capensis)muscle, with addition of microbial transglutaminase

AutorMoreno Conde, Helena María CSIC ORCID; Carballo, José CSIC ORCID ; Borderías, A. Javier CSIC ORCID
Palabras claveRestructured product
Physical properties
Protein quality
Microbial transglutaminase
Fish muscle
Fecha de publicación2009
EditorJohn Wiley & Sons
CitaciónJournal of the Science of Food and Agriculture 89: 1346- 1351 (2009)
ResumenBACKGROUND: Microbial transglutaminase (MTGase) can improve the mechanical and functional properties of restructured fish products without the need of thermal gelation. The present study seeks to determine whether, for different setting times, MTGase activity in restructured hake muscle made with pieces or with homogenised muscle can be affected by the quality of the protein in the raw materials. RESULTS: As regards mechanical properties, samples of both qualities subjected to the two different processes attained a suitable consistency after setting for 24 h at 5 No.C. The quality of the protein in the sample is important when pieces are used for restructuring, but not when sample is homogenised. Also, there were strong correlations between residual MTGase activity up to 12 h and mechanical properties and electrophoretic band density. Water binding capacity (WBC) was not significantly altered byMTGase addition. CONCLUSION: The experimental combination of 10 g kg-1 of MTGase, 15 g kg-1 of sodium chloride and 7.5 g kg-1 of sodium caseinate was suitable for the production of minimally processed raw restructured fish products made with two different qualities of fish protein and two different restructuring processes. In the restructured products made with pieces, the protein quality significantly affected final properties, but in finely homogenised product the protein quality was less important. © 2009 Society of Chemical Industry.
URIhttp://hdl.handle.net/10261/101997
DOI10.1002/jsfa.3592
Identificadoresdoi: 10.1002/jsfa.3592
issn: 0022-5142
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