Cryoprotective Effects of Lactitol, Palatinit and Polydextrose® on Cod Surimi Proteins during Frozen Storage

Abstract

The cryoprotective effects of lactitol dihydrate, Polydextrose@ and Palatinit (Isomalt) at 8% w/w in cod-surimi were compared to an industrial control containing a sucrose/sorbitol 1:l mixture and a control without additive. Surimi was stored at -20°C for 12 wk and examined for freeze-induced protein changes every 2 wk by salt extractable protein and differential scanning calorimetry analyses: Palatinit@, lactitol and Polydextrose@ stabilized surimi proteins equally well as did the sucrose/sorbitol mixture. Salt extractable protein and myosin peak enthalpy for surimi were maintained at the same level as the industrial control. Confirming earlier results, initial T,,-myosin yielded information regarding surimi protein stability over extended periods of frozen storage.

Cryoprotective effect of trehalose on washed chicken meat

“…Similar results was reported by Kijowski and Richardson (1996) for washed mechanically deboned poultry meat, this could be explained by concentration of myofibrillar protein by washing and different pH and ionic environment when compared to the raw state of muscle (Wright and Wilding 1984;Xiong et al 1987;Lesiow and Xiong 2001). Analysis of variance of myosin T p showed that myosin's T p varied significantly (P<0.05) as a function of mass fraction of trehalose, but not as of frozen storage time (Sych et al 1990;Herrera et al 2001) (Table 1). These shifts in T p of myosin to the higher values as the mass fraction of trehalose increases can be interpreted as a stabilization of myofibrillar proteins since a higher temperature was required to denature these proteins (Sych et al 1990;Sych et al 1991).…”

“…Analysis of variance of myosin T p showed that myosin's T p varied significantly (P<0.05) as a function of mass fraction of trehalose, but not as of frozen storage time (Sych et al 1990;Herrera et al 2001) (Table 1). These shifts in T p of myosin to the higher values as the mass fraction of trehalose increases can be interpreted as a stabilization of myofibrillar proteins since a higher temperature was required to denature these proteins (Sych et al 1990;Sych et al 1991). Highest shift in T p of myosin shows the samples of WCM mixed with 10% of trehalose for all storage time intervals.…”

“…1). Myofibrillar protein denaturation frozen storage expressed by the loss of protein solubility during is a result of formation of hydrogen or hydrophobic bonds, as well as disulfide bonds and ionic interaction (Sych et al 1990;MacDonald and Lanier 1991;Sych et al 1991;Auh et al 1999). …”

“…To protect myofibrillar proteins from freezedenaturation and during frozen storage and maintain its possibly high processability, cryoprotectants, such as disaccharides, polysaccharides, polyalcohol's, acids, polyphosphates are generally added (Park et al 1988;MacDonald and Lanier 1991). Most commonly used methods for determination cryoprotective effects of added substances are measurement of myofibrillar protein solubility SEP (Salt extractable protein), Ca 2+ ATP-ase activity, unfrozen water by Nuclear Magnet Resonance (NMR), and transition temperatures and enthalpy of myofibrillar proteins by Differential scanning calorimetry (DSC) (Sych et al 1990;Park 1994;Kijowski and Richardson 1996;Stangierski and Kijowski 2003;Day and Dora 2010;Nopianti et al 2011). Differential scanning calorimetry (DSC) is a useful technique for studying thermal behaviour of muscle proteins (Barbut and Findlay 1991).…”

Physico-chemical and thermal properties of chicken myofibrillar protein concentrate (CMPC) mixed with barley bran flour during frozen storage

“…AFS.2018.0537 processability (MacDonald et al, 2005). Measurements of myofibrillar protein solubility SEP (Salt extractable protein), Ca 2+ ATP-ase activity, unfrozen water by Nuclear Magnet Resonance (NMR), and transition temperatures and enthalpy of myofibrillar proteins by differential scanning calorimetry (DSC) are the most commonly used instrumental methods for the determination of the cryoprotective effects of added substances (Kijowski and Richardson, 1996;Park et al, 1993;Stangierski and Kijowski, 2008;Sych et al, 1990). DSC is an often used as instrumental method for studying thermal behaviour of muscle proteins (Findlay and Barbut, 1990).…”