Biochemical Properties of Actomyosin and Expressible Juice of Cold Stored Striated Adductor Muscles of Aulacomya ater ater (Molina):

Paredi, María E.; Mattio, Norma De Vido de; Crupkin, Marcos

doi:10.1300/j030v01n03_09

Cited by 5 publications

(8 citation statements)

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“…Preparation of Muscle Proteins. The procedure followed to obtain partially purified actomyosin was previously described (Paredi et al, 1990). Myofibrils were prepared by the procedure of Chantler and Szent-Gyorgyi (1980).…”

Section: Methodsmentioning

confidence: 99%

Thermal Denaturation of Muscle Proteins from Male and Female Squid (Illex argentinus) at Different Sexual Maturation Stages. A Differential Scanning Calorimetric Study

Paredi¹,

Tomás²,

Crupkin³

et al. 1996

J. Agric. Food Chem.

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The influence of both sex and sexual maturation stage of specimens on the thermal behavior of muscle proteins was investigated. Differential scanning calorimetry (DSC) thermograms of whole muscle of female squids showed four endothermic transitions [peak temperature maximum (T max), 45.9, 56.8, 67.2, and 79.2 °C]. The DSC thermograms of whole muscle of male squids showed three transitions (T max, 47.9, 56.8, and 79.2 °C). The T max of 67.2 °C, present only in female squid muscle, was related to sarcoplasmic proteins. Myosin and paramyosin contributed to the first transition, connective tissue to the second transition, and actin to the last transition. No major differences were observed in T max values that were related to the sex and sexual maturation stage of specimens. The lowest denaturation enthalpy (ΔH) was found in muscle from immature females. Independently of the sex and the sexual maturation stage of specimens, no major changes were observed in either T max or ΔH values during frozen storage of squids. Keywords: Squid muscle; thermal stability; myofibrillar proteins; sexual maturation stage; differential scanning calorimetry

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Section: Methodsmentioning

confidence: 99%

Thermal Denaturation of Muscle Proteins from Male and Female Squid (Illex argentinus) at Different Sexual Maturation Stages. A Differential Scanning Calorimetric Study

Paredi¹,

Tomás²,

Crupkin³

et al. 1996

J. Agric. Food Chem.

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“…Decreases of about 44% in both Mg 2+ -ATPase activity and reduced viscosity of actomyosin were observed after the first day of storage. Paredi et al (1992) found evidences of conformational changes in actomyosin from intrinsic viscosity and surface hydrophobicity determinations. The changes in the biochemical properties of actomyosin from muscles stored at 2-4 °C were accompanied by increases in the amounts of expressible juice.…”

Section: Introductionmentioning

confidence: 96%

Biochemical Properties of Actomyosin and Expressible Moisture of Frozen Stored Striated Adductor Muscles of Aulacomya ater ater (Molina): Effects of Polyphosphates

Paredi

Mattio

Crupkin

1996

J. Agric. Food Chem.

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Aulacomya adductor muscles with and without prior immersion in polyphosphates were frozen and stored at −30 °C. Expressible moisture of control samples increased after freezing and showed the highest increment at the second week of storage. Actomyosin extractability was not affected by freezing but decreased during frozen storage in both untreated and treated muscles. The reduced viscosity and the Mg2+-ATPase activity of actomyosin in dip-treatment free muscles fell with freezing and frozen storage. Polyphosphates reduced the amount of expressible moisture of the muscles and delayed the decrease in the enzymatic activity of actomyosin. Treatment with polyphosphates did not affect the viscosity of actomyosin. The relative percentages of myosin and paramyosin significantly decreased (p < 0.01) and those of actin significantly increased in actomyosin of both control and treated muscles at 4 weeks of frozen storage. These results would indicate that thin filaments in frozen striated adductor muscle are more stable than thick filaments. Keywords: Striated adductor muscles; myofibrillar proteins; biochemical properties; frozen storage; expressible moisture

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“…This would indicate that no aggregation took place in the first 24 h of storage. On the other hand, an increase in protein surface hydrophobicity of actomyosin from Aulacomya adductor muscle stored for up to 48 h was reported (Paredi et al, 1992). This result suggests that a weakening of hydrophobic interactions would occur earlier during postmortem storage.…”

Section: Resultsmentioning

confidence: 96%

“…A decrease of about 44% in both Mg2+-ATPase activity and reduced viscosity of actomyosin after the first day of storage were also reported. These changes were attributed to a conformational change of the protein by intrinsic viscosity and surface hydrophobicity determinations (Paredi et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Postmortem Changes in Adductor Muscles from Aulacomya ater ater (Molina) Stored at 2-4 .degree.C. A Differential Scanning Calorimetric Study

Paredi¹,

Tomás²,

Mattio³

et al. 1995

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Biochemical Properties of Actomyosin and Expressible Juice of Cold Stored Striated Adductor Muscles of Aulacomya ater ater (Molina):

Cited by 5 publications

References 0 publications

Thermal Denaturation of Muscle Proteins from Male and Female Squid (Illex argentinus) at Different Sexual Maturation Stages. A Differential Scanning Calorimetric Study

Thermal Denaturation of Muscle Proteins from Male and Female Squid (Illex argentinus) at Different Sexual Maturation Stages. A Differential Scanning Calorimetric Study

Biochemical Properties of Actomyosin and Expressible Moisture of Frozen Stored Striated Adductor Muscles of Aulacomya ater ater (Molina): Effects of Polyphosphates

Postmortem Changes in Adductor Muscles from Aulacomya ater ater (Molina) Stored at 2-4 .degree.C. A Differential Scanning Calorimetric Study

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