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Título: | Protein extracts and aggregates forming in minced cod (Gadus morhua) during frozen storage |
Autor: | Tejada Yábar, Margarita CSIC ; Careche, Mercedes CSIC ORCID ; Torrejón, Purificación; Mazo, M. Luisa del; Solas, M. Teresa; García, M. Luisa; Barba, Carlos | Palabras clave: | Microstructure Gadus morhua Mince Cod Actomyosin Frozen storage Aggregation |
Fecha de publicación: | 1996 | Editor: | American Chemical Society | Citación: | Journal of Agricultural and Food Chemistry 44: 3308-3314 (1996) | Resumen: | Natural actomyosin was extracted from frozen minced cod muscle stored for up to 62 weeks at -20 °C with 0.6 M NaCl, and the insoluble aggregates, when formed, were solubilized successively with 2% sodium dodecyl sulfate (SDS) and 2% SDS + 5% β-mercaptoethanol (ME) solutions, giving extracted fractions S1 (NaCl), S2 (SDS), and S3 (ME + SDS), precipitates insoluble in 0.6 M NaCl (P1) and 2% SDS (P2), and a precipitate not soluble in any of the agents used (P3). SDS polyacrylamide gel electrophoresis (SDS-PAGE) of fraction S1 showed that the proportion of the major proteins changed during frozen storage. Size exclusion chromatography snowed a decrease in the peak containing myosin heavy chain (MHC) and actin (Ac). Transmission electron microscopy (TEM) of S1 showed at the outset a filamentous morphology associated with globules interconnected crosswise. As storage progressed, the number and size of aggregates increased. In fractions S2 and S3, the major proteins detected by SDS-PAGE were MHC and Ac. TEM showed a greater abundance of ring-shaped structures than in S1. TEM of the insoluble fractions showed a sarcomerelike structure, more pronounced the milder the solubilizing treatment and the longer the storage time. | Versión del editor: | https://doi.org/10.1021/jf960158w | URI: | http://hdl.handle.net/10261/94617 | DOI: | 10.1021/jf960158w | Identificadores: | issn: 0021-8561 |
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