Chemical Deterioration of Muscle Proteins During Frozen Storage

Matsumoto, Juichiro J.

doi:10.1021/bk-1980-0123.ch005

Cited by 120 publications

(104 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, fish proteins undergo changes during frozen storage as a result of denaturation, dissociation and aggregation, which changes are evident as variations in texture (Chu and Sterling 1970;Sikorski et ~1 1 9 7 6 ;Gill ef af 1979;Tejada 1979;Matsumoto 1980;Shenouda 1980;Careche 1988 The purpose here was to study the FC of fish muscle during frozen storage with reference to the lipid content of the species and the season of capture.…”

Section: Introductionmentioning

confidence: 99%

Foaming capacity of fish minces during frozen storage

Huidobro

Tejada

1992

J Sci Food Agric

View full text Add to dashboard Cite

This work covers a year's study of the foaming capacity (FC) of minced muscle of three fish species-blue whiting (Micromesistius poutussou R), horse mackerel (Trachurus truchurus L), and mackerel (Scomber scombrus LFcaught in two different seasons (January and July) and stored at -18°C. Periodic assays were performed to determine protein solubility, FC and dimethylamine formation.The results show that FC is initially inhibited by the presence of the species own lipids; however, during frozen storage this effect is attenuated and thus FC increases. The results corroborate the view that protein solubility is not an indispensible requisite for FC, and that mere dispersion of proteins is sufficient. However, FC is not diminished by changes in protein during frozen storage when this deficiency is offset by sufficient protein concentration. On the other hand, FC is clearly affected by the formaldehyde generated during frozen storage, so that beyond a certain level the aggregates formed as a result of formaldehyde formation are too large to disperse, and hence FC decreases drastically.

show abstract

Section: Introductionmentioning

confidence: 99%

Foaming capacity of fish minces during frozen storage

Huidobro

Tejada

1992

J Sci Food Agric

View full text Add to dashboard Cite

show abstract

“…of denaturation (aggregation) of a-helical proteins during frozen storage and its prevention by cryprotectants. -Ef), catiornc side chain; -9, amonie side chain; -0, nonpolar side chain; @, water molecule; 8-9, dianiornc cryoprotectant molecule (from Matsumoto, 1980).…”

mentioning

confidence: 99%

“…A hypothetical mechanism of freeze denaturation in non-helical proteins and hs prevention by cryoprotectants was proposed by Matsumoto (1980) (Figure 2.8). When a globular or non-helical protein dissolved in water, the conformation of the native globular molecule is maintained largely by the intramolecular non-polar bonds, which have resulted from a thermodynamic balance between the two systems, A and B.…”

mentioning

confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

View full text Add to dashboard Cite

: The changes in protein structure associated with the preparation and frozen storage of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at ‐20 °C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the a‐helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native‐PAGE showed no major changes in surimi after 24 mo storage at ‐20 °C. FTIR/ ATR spectroscopy indicated a significant decrease in a‐helix relative to p‐sheet structure in surimi after 2 y of storage at ‐20 °C. The loss of α‐helical content was more significant in slowly frozen surimi compared with rapid‐frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.

show abstract

“…Basically two theories pertain to the cryoprotective activity of compounds with low molecular weights. Naguchi and Matsumoto [11,13] suggested that functional groups of these compounds are bound via hydrogen bonds with the active groups of molecules of the preserved protein.…”

Section: Introductionmentioning

confidence: 99%

Effect of selected commercial substances with cryoprotective activity on the quality of mechanically recovered, washed and frozen stored poultry meat

Stangierski¹,

Kijowski²

2003

Nahrung

View full text Add to dashboard Cite

Investigations were conducted on mechanically recovered poultry meat (MRPM) and on protein preparation obtained from MRPM by washing it first with 1% water solution of sodium chloride and with water afterwards. The raw materials were frozen at the temperature of -23 C. The effect of added stabilizers on the quality of gels produced from fresh raw materials, and after freezing and frozen storage was assessed. The following additives were used: 1% pork hydrolizate (Pork Stock), 0.5% Cremodan containing carrageens, and 1.5% bovine blood plasma (AMP 600N). Freezing and frozen storage caused a significant reduction of functional properties of MRPM and its protein preparation. None of the examined additives protected simultaneously all the investigated functional properties of the frozen samples. The amount of thermal drip, the gel texture and the amount of protein transition heat were determined by scanning differential calorimetry. The lowest thermal drip in gels obtained from frozen-stored samples was observed when bovine blood plasma was used as a stabilizer. On the other hand, the most advantageous protective effect on the proteins of the frozen MRPM and on the preparation, determined by mechanical strain resistance of the gels, was found with 1% pork hydrolizate added. The results of thermodynamic investigations of proteins revealed that the best protective effect on the frozen preparation was observed with 1.5% blood plasma added. No protective activity of added Cremodan on proteins of the frozen protein preparation was noted.

show abstract

Chemical Deterioration of Muscle Proteins During Frozen Storage

Cited by 120 publications

References 0 publications

Foaming capacity of fish minces during frozen storage

Foaming capacity of fish minces during frozen storage

Protein Structural Changes During Preparation and Storage of Surimi

Effect of selected commercial substances with cryoprotective activity on the quality of mechanically recovered, washed and frozen stored poultry meat

Contact Info

Product

Resources

About