EVALUATION OF PROTEIN FUNCTIONALITY IN ALKALI AND NONALKALI SURIMI PROCESSED MECHANICALLY DEBONED CHICKEN MEAT<sup>1</sup>

Yang, Tianyu; Froning, G. W.

doi:10.1111/j.1745-4573.1994.tb00532.x

Cited by 13 publications

(13 citation statements)

References 15 publications

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“…The values of peak thermal temperatures (t p ) of myosin and actin were different then the values of beef meat reported by Barbut and Findlay (1991), Bircan and Barringer (2000), and Brunton et al (2006). 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).…”

Section: Differential Scanning Calorimetrysupporting

confidence: 55%

“…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 et al 1993;Park 1994;Yang & Froning 1994;Kijowski & Richardson 1996;Stangierski & Kijowski 2003). Differential scanning calorimetry (DSC) is a useful technique for studying the thermal behaviour of muscle proteins (Barbut & Findlay 1991).…”

Section: Camentioning

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 Calorimetrysupporting

confidence: 55%

Section: Camentioning

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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“…The denaturation temperatures (T p ) of myosin and actin were different from the denaturation temperatures of chicken meat reported by by Barbut and Findlay (1991) and Bircan and Barringer (2002). 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).…”

Section: Thermal Analysissupporting

confidence: 47%

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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“…The 0.5 % sodium bicarbonate washing solution provides better heme pigment extraction due to the solubilization of the muscle sarcoplasmic proteins Froning 1992, 1994;Maza 2001;Ensoy et al 2004), but may adversely affect functionality of myofibrillar proteins (Yang and Froning 1994). Addition of 0.5 % sodium bicarbonate solution resulted in a product with the highest pH, lowest fat and lowest pigment concentration, all of which are favorable characteristics in the manufacturing of further processed products (Ismail et al 2011).…”

Section: Compositional Properties Of Mscm and Mscm Surimi-like Materialsmentioning

confidence: 99%

Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology

2013

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Surimi is a semi-processed washed fish mince protein concentrate mixed with cryoprotectants for frozen storage, which is the primary constituent of processed foods. Mechanically separated chicken meat (MSCM) is a common ingredient of comminuted sausages mainly due to its low price. The present work aimed to define the adequate parameters to obtain surimi-like material from MSCM using response surface methodology, and to characterize the chemical and textural properties of this product. The MSCM was utilized in the elaboration of surimi-like material using the bleaching method with sodium bicarbonate and sodium chloride solutions. For this purpose, the effect of process parameters viz: temperature (T=2, 7, and 12°C), time (t=5, 10, and 15 min/cycles) and washing solution:MSCM ratio (R=2:1, 4:1, and 6:1w/w) were evaluated using response surface methodology. The highest composite design averages obtained were 10.7 % for protein content, 1,003.4 g for breaking force, 645.8 g.cm for gel strength, 9.0 N for cutting strength, and 24.1 N.s for work of shearing at the optimum combination of processing conditions of 7°C, 10 min and 4:1 washing solution:MSCM ratio, corresponding to the central points of the proposed experimental design. The obtained models had high determination coefficients, explaining 95.85, 98.23, 98.41, and 96.08 % of total variability in protein content, cutting strength, breaking force, and work of shearing variabilities, respectively. According to the folding test the surimi-like material presented the same characteristics of a high quality surimi (FT=5).

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EVALUATION OF PROTEIN FUNCTIONALITY IN ALKALI AND NONALKALI SURIMI PROCESSED MECHANICALLY DEBONED CHICKEN MEAT¹

Cited by 13 publications

References 15 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

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

Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology

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EVALUATION OF PROTEIN FUNCTIONALITY IN ALKALI AND NONALKALI SURIMI PROCESSED MECHANICALLY DEBONED CHICKEN MEAT1

Cited by 13 publications

References 15 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

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

Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology

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EVALUATION OF PROTEIN FUNCTIONALITY IN ALKALI AND NONALKALI SURIMI PROCESSED MECHANICALLY DEBONED CHICKEN MEAT¹