Protein Extracts and Aggregates Forming in Minced Cod (Gadus morhua) during Frozen Storage
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- 作者：M. Tejada ; M. Careche ; P. Torrejó ; n ; M. L. del Mazo ; M. T. Solas ; M. L. Garcí ; a ; and C. Barba
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：1996
- 出版时间：October 1996
- 年：1996
- 卷：44
- 期：10
- 页码：3308 - 3314
- 全文大小：440K
- 年卷期：v.44,no.10(October 1996)
- ISSN：1520-5118
文摘
Natural actomyosin was extracted from frozen minced cod muscle storedfor up to 62 weeks at -20
C with 0.6 M NaCl, and the insoluble aggregates, when formed, weresolubilized successively with2% sodium dodecyl sulfate (SDS) and 2% SDS + 5%
-mercaptoethanol (ME) solutions, givingextracted 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 theagents used (P3). SDSpolyacrylamide gel electrophoresis (SDS-PAGE) of fraction S1 showedthat the proportion of themajor proteins changed during frozen storage. Size exclusionchromatography showed a decreasein the peak containing myosin heavy chain (MHC) and actin (Ac).Transmission electron microscopy(TEM) of S1 showed at the outset a filamentous morphology associatedwith globules interconnectedcrosswise. As storage progressed, the number and size ofaggregates increased. In fractions S2and S3, the major proteins detected by SDS-PAGE were MHC and Ac.TEM showed a greaterabundance of ring-shaped structures than in S1. TEM of theinsoluble fractions showed a sarcomere-like structure, more pronounced the milder the solubilizing treatmentand the longer the storagetime.Keywords: Aggregation; frozen storage; actomyosin; cod; mince; Gadusmorhua; microstructure
C with 0.6 M NaCl, and the insoluble aggregates, when formed, weresolubilized successively with2% sodium dodecyl sulfate (SDS) and 2% SDS + 5%-mercaptoethanol (ME) solutions, givingextracted 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 theagents used (P3). SDSpolyacrylamide gel electrophoresis (SDS-PAGE) of fraction S1 showedthat the proportion of themajor proteins changed during frozen storage. Size exclusionchromatography showed a decreasein the peak containing myosin heavy chain (MHC) and actin (Ac).Transmission electron microscopy(TEM) of S1 showed at the outset a filamentous morphology associatedwith globules interconnectedcrosswise. As storage progressed, the number and size ofaggregates increased. In fractions S2and S3, the major proteins detected by SDS-PAGE were MHC and Ac.TEM showed a greaterabundance of ring-shaped structures than in S1. TEM of theinsoluble fractions showed a sarcomere-like structure, more pronounced the milder the solubilizing treatmentand the longer the storagetime.Keywords: Aggregation; frozen storage; actomyosin; cod; mince; Gadusmorhua; microstructure