Characteristics of the Salt-Soluble Fraction of Hake (Merluccius merluccius) Fillets Stored at -20 and -30 C
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- 作者：M. Luisa del Mazo ; Purificació ; n Torrejó ; n ; Mercedes Careche ; and Margarita Tejada
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：1999
- 出版时间：April 1999
- 年：1999
- 卷：47
- 期：4
- 页码：1372 - 1377
- 全文大小：129K
- 年卷期：v.47,no.4(April 1999)
- ISSN：1520-5118
文摘
Natural actomyosin (NAM) extracted in 0.6 M NaCl from hake fillets stored at -20 and -30 
C forup to 49 weeks was studied. The extracted protein decreased as storage progressed and becamepoorer in myosin while the proportion of actin remained constant. Two major peaks composed ofmyosin plus actin and actin plus tropomyosin plus troponins were obtained by size exclusion chromatography. SDS-PAGE analysis of the protein retained in the precolumn filter showed that therewas protein aggregated by covalent bonding. Surface hydrophobicity increased while Ca2+-ATPaseactivity, apparent viscosity, and SH groups decreased as storage progressed. The loss of Ca2+-ATPaseactivity was due mainly to denaturation of the extracted myosin, whereas the minimum viscosityvalues occurred earlier and were not directly due to the lower proportion of myosin in the extracts.Thus, the extracted NAM exhibited changes during frozen storage. The temperature-dependentdifference was mainly quantitative due to a smaller amount of protein extracted at -20 C.Keywords: Hake; fillets; frozen storage; salt soluble; functionality; actomyosin
C forup to 49 weeks was studied. The extracted protein decreased as storage progressed and becamepoorer in myosin while the proportion of actin remained constant. Two major peaks composed ofmyosin plus actin and actin plus tropomyosin plus troponins were obtained by size exclusion chromatography. SDS-PAGE analysis of the protein retained in the precolumn filter showed that therewas protein aggregated by covalent bonding. Surface hydrophobicity increased while Ca2+-ATPaseactivity, apparent viscosity, and SH groups decreased as storage progressed. The loss of Ca2+-ATPaseactivity was due mainly to denaturation of the extracted myosin, whereas the minimum viscosityvalues occurred earlier and were not directly due to the lower proportion of myosin in the extracts.Thus, the extracted NAM exhibited changes during frozen storage. The temperature-dependentdifference was mainly quantitative due to a smaller amount of protein extracted at -20 C.Keywords: Hake; fillets; frozen storage; salt soluble; functionality; actomyosin