Aggregation of Myofibrillar Proteins in Hake, Sardine, and Mixed Minces during Frozen Storage

Huidobro, Almudena; Mohamed, Gamal Fouad; Tejada, Margarita

doi:10.1021/jf970962y

Cited by 15 publications

(15 citation statements)

References 22 publications

(22 reference statements)

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“…1987). However, fish muscle deteriorates during frozen storage mainly because of the denaturation and aggregation of myofibrillar proteins (Huidobro et al. 1998).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical and Biochemical Changes in Whole Lizardfish (Saurida Micropectoralis) Muscles and Fillets During Frozen Storage

Leelapongwattana

Benjakul

Visessanguan

et al. 2005

J Food Biochemistry

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The physicochemical and biochemical changes in whole lizardfish (Saurida micropectoralis) muscles and its fillets kept in air and under vacuum during frozen storage at −20C for 24 weeks were investigated. The formaldehyde (FA) and dimethylamine contents increased with a concomitant decrease in trimethylamine‐ N‐oxide (TMAO) content as the storage time increased (P < 0.05). The Ca2+–adenosine 5′‐triphosphatase activity continuously decreased with a coincidental decrease in salt‐soluble fraction. The disulfide bonds were increasingly formed throughout the storage (P < 0.05). The surface hydrophobicity increased and reached the maximum at week 12 with a subsequent decrease up to the end of storage. In general, the higher changes were observed in samples kept under vacuum than those kept in air. With the same atmosphere used, the whole fish showed slightly higher changes than the fillets. A marked increase in TMAO demethylase (TMAOase) activities was observed up to 12 weeks, followed by the continuous decrease up to 24 weeks of storage. The produced FA might play an important role in inducing protein denaturation and/or aggregation in lizardfish. The TMAOase activity as well as the FA formation could be reduced to some extent with the removal of internal organs and storage in the presence of oxygen. However, a detrimental effect of oxygen, especially on the promotion of lipid oxidation, would be an obstacle.

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“…1987). However, fish muscle deteriorates during frozen storage mainly because of the denaturation and aggregation of myofibrillar proteins (Huidobro et al. 1998).…”

Section: Introductionmentioning

confidence: 99%

Physicochemical and Biochemical Changes in Whole Lizardfish (Saurida Micropectoralis) Muscles and Fillets During Frozen Storage

Leelapongwattana

Benjakul

Visessanguan

et al. 2005

J Food Biochemistry

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“…Natural actomyosin was extracted with 0.6 M NaCl from 100 g mince samples according to the method of Kawashima et al 20 as described by Huidobro et al 8 The concentration of protein in the extracts was determined by the Lowry method 21 and confirmed by the Kjeldahl method. 22 The extractability of natural actomyosin was expressed as mg NAM g −1 protein in the muscle.…”

Section: Natural Actomyosin Extractionmentioning

confidence: 99%

“…3,9 The changes in the extracted NAM during frozen storage are also consistent with the type of aggregates that form in these species during frozen storage and are unextractable in salt solutions. 8 Mixing of varying amounts of hake and sardine minces altered the amount, type and appearance of the NAM extracted. The incidence of aggregates formed by ring-shaped structures increased with time in all cases.…”

Section: Transmission Electron Microscopy Of Natural Actomyosinmentioning

confidence: 99%

“…Nevertheless, the amount of protein linked by covalent bonds increases with time. 8 In the mixed lots the morphology of the extracts changed in accordance with the amount of sardine and the length of storage time. In lots with 50% sardine the TEM images of the extracts obtained after 2 months of frozen storage resembled those of hake, but with aggregates increasing in line with the percentage of sardine.…”

Section: Emulsifying Propertiesmentioning

confidence: 99%

“…19 Addition of sardine minces to hake minces also changed the type of protein aggregate that became unextractable in salt solutions during frozen storage. 8 Many functional properties of proteins have been related to solubility or extractability of the myofibrillar fraction.…”

Section: Introductionmentioning

confidence: 99%

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Effect of frozen storage of hake, sardine and mixed minces on natural actomyosin extracted in salt solutions

et al. 2003

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Natural actomyosin extracted in salt solutions from mixtures of hake and sardine minces (3:1; 1:1 and 1:3 w/w) stored frozen for up to 1 year differed in the amount extracted and in the characteristics of the extracts. In the mixed minces the amount of natural actomyosin extracted decreased during frozen storage at a higher rate than that theoretically corresponding to the amount of hake in the mixes. With increasing storage time and proportion of sardine a lower percentage of myosin heavy chain and actin was observed by electrophoresis. An increased size of aggregates was also observed by electrophoresis and transmission electron microscopy. The stability of emulsions was enhanced when aggregates appeared in the extracts. The decrease in the amount of natural actomyosin extracted does not explain the changes observed in the texture of the minces during frozen storage. This may indicate that the size of the aggregates unextractable in salt solutions, independently of the type of bonds that bind the proteins in the aggregates, plays an important role in the textural changes observed. Copyright © 2003 Society of Chemical Industry

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Addition of sardine to hake minces and subsequent effect on dimethylamine and formaldehyde formation

Tejada¹,

Mohamed²,

Huidobro³

2002

J Sci Food Agric

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Formaldehyde formation and reaction with muscle proteins in lean fish species during frozen storage is considered to be a major factor affecting texture and functionality deterioration. Formaldehyde formation and reaction with muscle compounds was reduced in lean fish minces and model systems when lipids with different degrees of oxidation were added. In order to increase the lipid content and slow down functional and textural changes, hake (Merluccius merluccius) and sardine (Sardina pilchardus) minces mixed in the ratios 3:1; 1:1 and 1:3 (w/w) were stored at −20 °C and studied for 1 year. Dimethylamine formation and, by deduction, formaldehyde formation increased. However, less free formaldehyde was detected, probably owing to reaction with muscle compounds in the mixed minces. Nevertheless, addition of sardine minces improved the texture, protein solubility and viscosity of the mixed minces compared with the hake minces. In the mixed lots, formation of large protein aggregates was delayed or prevented. This suggests that in the mixed minces formaldehyde reacted with proteins in a different way from that in lean fish or reacted with other muscle components not directly involved in textural changes.© 2002 Society of Chemical Industry

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Aggregation of Myofibrillar Proteins in Hake, Sardine, and Mixed Minces during Frozen Storage

Cited by 15 publications

References 22 publications

Physicochemical and Biochemical Changes in Whole Lizardfish (Saurida Micropectoralis) Muscles and Fillets During Frozen Storage

Physicochemical and Biochemical Changes in Whole Lizardfish (Saurida Micropectoralis) Muscles and Fillets During Frozen Storage

Effect of frozen storage of hake, sardine and mixed minces on natural actomyosin extracted in salt solutions

Addition of sardine to hake minces and subsequent effect on dimethylamine and formaldehyde formation

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