Highly Concentrated Branched Oligosaccharides as Cryoprotectant for Surimi

Auh, Joong-Hyuck; Lee, H. G.; Kim, J. W.; Yoon, Hae-Sung; Park, K. H.

doi:10.1111/j.1365-2621.1999.tb15055.x

Cited by 47 publications

(37 citation statements)

References 23 publications

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“…Carvajal et al (1999) revealed the ability of maltodextrins of varying mean molecular weight (versus sucrose or a sucrose-sorbitol mixture) to stabilize Alaska pollock surimi proteins to the denaturing effects of frozen storage. Furthermore, highly concentrated branched oligosaccharides were used as cryoprotectants for surimi by other researchers (Auh et al, 1999).…”

Section: Stabilization Of Protein In Surimimentioning

confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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: 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.

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Section: Stabilization Of Protein In Surimimentioning

confidence: 99%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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“…Myofibrillar protein denaturation during frozen storage expressed by the loss of protein solubility is a result of hydrogen or hydrophobic bonds formation, as well as of that of disulfide bonds, and of ionic interactions (Sych et al 1990(Sych et al , 1991MacDonald & Lanier 1991;Auh et al 1999). SEP of WBM decreased quasi linearly as a function of storage time.…”

Section: Salt Soluble Proteins (Sep)mentioning

confidence: 99%

Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat

Kovačević¹,

Mastanjević²

2011

Czech J. Food Sci.

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Kovačević D., Mastanjević K. (2011): Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat. Czech J. Food Sci., 29: 15-23.The cryoprotective effects of trehalose and maltose (w = 2-10%) on washed beef meat were investigated. Washed beef meat produced from fresh beef meat was frozen and stored for 360 days at -30°C. Myofibrillar protein functional stability was monitored by salt extractable protein (SEP) and differential scanning calorimetry (DSC). Salt extractable protein (SEP) showed that the addition of trehalose and maltose causeda smaller loss of protein solubility during the frozen storage. Peak thermal transition (t p ) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in the peak thermal transition temperature (t p ) of myosin and actin to higher temperature as the mass fractions of trehalose and maltose increased. The transitions enthalpies of myosin and actin of the washed beef meat samples showed a higher increase with the increase of mass fraction of trehalose then of that of maltose. Since the value of denaturation enthalpy is directly related to the amount of native proteins, higher values of ΔH point to higher cryoprotective effects of trehalose.

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“…A cryoprotectant is a substance that is used to protect biological tissue from freezing damage, which has been reported to slow down the rate of ice crystal growth and alter crystal shapes (Sych et al 1990 andAlvarez et al 2010). The most commonly used cryoprotectants in the surimi industry have been low molecular weight sugars and polyols, such as sucrose and/or sorbitol, typically added at 8% (w/w) alone or in mixture 1:1 to leached fish muscle (Auh et al 1999). Therefore, the objective of this study was to investigate the effect of cryoprotectants composition on physico-chemical characteristics of spent laying hen breast surimi for improvement of unpopular meat consumption.…”

Section: Introductionmentioning

confidence: 99%

Effect of Cryoprotectants on Chemical, Mechanical and Sensorial Characteristics of Spent Laying Hen Surimi

Jin

Kim

Jung

et al. 2010

Food Bioprocess Technol

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The surimi samples were divided into four groups (C, surimi made from Alaska pollack by water washing with NaCl-free cryoprotectant; T1, made from spent laying hen breast by water washing with NaCl-free cryoprotectant; T2, made from spent laying hen breast by water washing with NaCl and sugar-free cryoprotectant; T3, made from spent laying hen breast by water washing with NaCl-contained cryoprotectant). In proximate compositions, collagen and myofibrillar protein were significantly higher in spent laying hen breast surimi samples (T1, T2, and T3) than Alaska pollack surimi sample (C). Folding test score was significantly higher in T3 in all storage periods. Spent laying hen breast surimi samples (T1, T2, and T3) had higher lighness (L*) and whiteness (W) than Alaska pollack surimi sample (C) in all storage period. In sensory evaluation, T3 showed significantly higher score in all sensory evaluation items. As a result of study, the qualities of T3 are higher than those of other surimi samples.

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Highly Concentrated Branched Oligosaccharides as Cryoprotectant for Surimi

Cited by 47 publications

References 23 publications

Protein Structural Changes During Preparation and Storage of Surimi

Protein Structural Changes During Preparation and Storage of Surimi

Cryoprotective effect of trehalose and maltose on washed and frozen stored beef meat

Effect of Cryoprotectants on Chemical, Mechanical and Sensorial Characteristics of Spent Laying Hen Surimi

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