Mechanism of Rheological Changes in Poultry Myofibrillar Proteins During Gelation

Lesiów, Tomasz; Xiong, Youling L.

doi:10.3184/147020601783698486

Cited by 36 publications

(22 citation statements)

References 32 publications

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“…Values of denaturation temperatures (T p ) of myosin and actin were different then values of raw chicken breast meat reported by Kijowski and Mast (1988), Murphy et al (1998) and Bircan and Barringer (2002). 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).…”

Section: Differential Scanning Calorimetrysupporting

confidence: 74%

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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Section: Differential Scanning Calorimetrysupporting

confidence: 74%

Cryoprotective effect of trehalose on washed chicken meat

Kovačević¹,

Mastanjević²

2011

J Food Sci Technol

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“…Similar results were reported by Yang and Froning (1994), and Kijowski and Richardson (1996) for washed mechanically deboned poultry meat. This could be explained by the concentration of myofibrillar protein through washing and different pH and ionic environment when compared to the raw state of muscle (Wright & Wilding 1984;Xiong et al 1987;Lesiow & Xiong 2001). The analysis of variance of myosin t p showed that myosin t p varied significantly (P < 0.05) as a function of the mass fraction of trehalose, but not as that of frozen storage time (Sych et al 1990) ( Table 2).…”

Section: Differential Scanning Calorimetrymentioning

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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“…Yang and Froning (1994) and Kijowski and Richardson (1996) reported similar results for washed mechanically-deboned poultry meat. This could be related to by concentration of myofibrillar proteins by washing, and the different pH and ionic environment when compared to the raw state of muscle (Lesiow and Xiong, 2001). Myosin's T p varied significantly (p < 0.05) as a function of mass fraction of barley bran flour, but not as a function of frozen storage time (Table 1).…”

Section: Thermal Analysismentioning

confidence: 99%

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

Mastanjević¹,

Kovačević²

2018

Acta Sci Pol Technol Aliment

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Chicken myofibrillar protein concentrate (CMPC), produced with modified technology used for fish surimi (Dawson et al., 1988;Park et al., 1996), is characterized by very good technological properties, such as a high water retention capacity and a strong ability to form strong gels after being heated. The most frequently used food preservation technique for this kind of product is freezing. Cryoprotectants, such as disaccharides, polysaccharides, polyalcohols, acids and polyphosphates are generally added to surimi to protect myofibrillar proteins from freeze-denaturation during frozen storage and to maintain its high PHYSICO-CHEMICAL AND THERMAL PROPERTIES OF CHICKEN MYOFIBRILLAR PROTEIN CONCENTRATE (CMPC) MIXED WITH BARLEY BRAN FLOUR DURING FROZEN STORAGE ABSTRACTBackground. Possible new additives for surimi-like products made from chicken meat, which could improve its functional properties during frozen storage, are the subject of much research. The use of dietary fibre in surimi-like products made from chicken meat has not been extensively studied. The objective of this study was to determine the effectiveness of barley bran flour in stabilizing chicken myofibrillar proteins during frozen storage and maintaining its functionality. Material and methods. Surimi-like material (chicken myofibrillar protein concentrate -CMPC) from mechanically deboned chicken meat was mixed with barley bran flour (0-6%) and stored in a freezer for 30, 60, 90 and 180 days. Instrumental color measurements (L*, a*, and b* values) were taken using a Hunter-Lab Mini ScanXE. Texture profile analysis (TPA) tests were performed using a TA.XT2i SMS Stable Micro Systems Texture Analyzer) equipped with an aluminium cylindrical probe P/75. Differential scanning calorimetry (DSC) was used for the determination of denaturation temperatures and enthalpies.Results. Denaturation enthalpies of CMPC increased when the mass fraction of barley bran was increased (w = 0-6%). Instrumental color parameters (L*, a* and b*) of CMPC gels were significantly (p < 0.05) affected by the addition of barley bran. Texture profile analysis (TPA) parameters -hardness and chewinessincreased significantly (p < 0.05) with the addition of barley bran (w = 0-6%). Cohesiveness and springiness were also significantly (p < 0.05) affected by the addition of barley bran (w = 0-6%) during frozen storage. Conclusion. The increase in denaturation enthalpies and some instrumental textural and color parameters, indicate possible interactions of chicken myofibrillar proteins with barley bran.

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Mechanism of Rheological Changes in Poultry Myofibrillar Proteins During Gelation

Cited by 36 publications

References 32 publications

Cryoprotective effect of trehalose on washed chicken meat

Cryoprotective effect of trehalose on washed chicken meat

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

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

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