Determination of Optimal Level of Lactitol for Surimi

Sych, J.; Lacroix, Christophe; Carrier, Marie‐Claude

doi:10.1111/j.1365-2621.1991.tb05263.x

Cited by 24 publications

(17 citation statements)

References 17 publications

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“…t p of myosin of WBM samples mixed with maltose varied significantly (P < 0.05) as a function of the mass fraction of trehalose and as a function of time (Table 3) (Herrera et al 2001). These shifts in t p of myosin to higher values as the mass fraction of trehalose and maltose increases can be interpreted as stabilisation of myofibrillar proteins since a higher temperature is required to denature these proteins (Sych et al 1990(Sych et al , 1991. The highest shift in myosin t p was shown by the samples of WBM mixed with 10% of trehalose for all storage time intervals.…”

Section: Differential Scanning Calorimetrymentioning

confidence: 98%

“…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%

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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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Section: Differential Scanning Calorimetrymentioning

confidence: 98%

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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show abstract

“…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.…”

Section: Differential Scanning Calorimetrymentioning

confidence: 99%

“…T p of actin transitions vary significantly (P<0.05) with addition of trehalose but not with frozen storage time (Table 1). T p of myosin shows higher shift by increase of mass fraction of trehalose then a T p of actin for all samples and all time intervals (Table 1) (Sych et al 1990;Sych et al 1991). The method of expressing peak enthalpies ΔH was adopted to provide an estimate of the quantity of native proteins.…”

Section: Differential Scanning Calorimetrymentioning

confidence: 99%

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Cryoprotective effect of trehalose on washed chicken meat

Kovačević¹,

Mastanjević²

2011

J Food Sci Technol

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The cryoprotective effects of trehalose (w=0-10%) on washed chicken meat (WCM) were investigated. WCM was produced from broiler, frozen and stored for 360 days on −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 caused smaller decrease in protein solubility during frozen storage. Peak thermal transition (T p ) and denaturation enthalpy (ΔH) of myofibrillar proteins were evaluated. Differential scanning calorimetry (DSC) revealed a shift in peak thermal transition temperature (T p ) of myosin and actin to higher temperature as the mass fraction of trehalose increases. The transitions enthalpies of myosin and actin of WCM samples showed higher increase with the increase of mass fraction of trehalose. Since the value of denaturation enthalpy is directly related to amount of native proteins, higher values of ΔH indicates to the higher cryoprotective effects of trehalose.

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Differential Scanning Calorimetry

Schubring

2009

Fishery Products

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Differential scanning calorimetry (DSC) is a well-established measuring method that is used on a large scale in different areas of research, development, and quality inspection and testing. Thermal effects can be quickly identifi ed and the relevant temperature and the characteristic caloric values determined using substance quantities in the mgmilligram range. Measurement values obtained by DSC allow heat capacity, heat of transition kinetic data, purity and glass transition to be determined. DSC curves serve to identify substances (Höhne et al. 1996). When a material undergoes a change in physical state such as melting or transition from one crystalline form to another, or when a material reacts chemically, heat is either absorbed or liberated. According to Lund (1983), DSC offers a tremendous potential for studying physicochemical changes that occur in foods. During the 1980s, its use in food research became apparent.DSC is characterised by its usefulness for analysing phase changes. Reactions that can lead to such phase changes are crystallisation of water (melting and freezing), evaporation of water and certain chemical reactions, for example protein denaturation. In DSC the temperature of the sample and reference are maintained the same and amount of heat required to achieve this is recorded. The DSC curve is a plot of heat fl ow against temperature. Consequently, the enthalpy change involved in the reaction can be determined from the area under the curve of heat-fl ow versus time. Material of known enthalpy can be used to calibrate the equipment. For samples containing water, evaporation is prevented using sealed containers. For examining frozen water in foods, results that are more reproducible are obtained while thawing frozen products than during cooling and freezing of products, because the variable phenomenon of super-cooling occurs during freezing. For proteins, the temperature corresponding to the maximum peak height is often used as an indication of the denaturation temperature, and the width of the peak as a measure of the complexity of the denaturation reaction. Using these assumptions, it is possible to observe how the denaturation temperature is affected by the changes in pH or the presence of other components, and the variation in enthalpy with denaturation temperature. As a protein becomes more denatured, the size of the peak should decrease. Phase changes in these both main components of the fi sh fl esh (water and protein) are subject of DSC investigation in this special fi eld. DSC has emerged 173 Fishery Products: Quality, safety and authenticity Edited by Hartmut Rehbein and Jörg Oehlenschläger

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Determination of Optimal Level of Lactitol for Surimi

Cited by 24 publications

References 17 publications

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

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

Cryoprotective effect of trehalose on washed chicken meat

Differential Scanning Calorimetry

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