The mechanism of high pressure-induced gels of rabbit myosin

Cao, Yingying; Xia, Tianlan; Zhou, Guanghong; Xu, Xinglian

doi:10.1016/j.ifset.2012.04.005

Cited by 137 publications

(67 citation statements)

References 42 publications

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“…Surface hydrophobicity ANS (1-anilinonaphthalene-8-sulphonic acid) as a hydrophobic fluorescence probe had a relatively weak fluorescence when dispersed in water, while its fluorescence increased dramatically when bound to non-polar parts (hydrophobic sites or pockets) of protein molecules (Cao et al, 2012). The increase of hydrophobicity of protein was caused by the exposure of the interior hydrophobic residues of protein molecules (Chan et al, 1992).…”

Section: Resultsmentioning

confidence: 99%

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

Zhang

Yang

Tang

et al. 2015

FSTR

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IntroductionFunctional properties of heat-induced myofibrillar protein gel were important for meat products (Fukazawa et al., 1961;Macfarlane et al., 1977;Siegel and Schmidt, 1979). Gel formation was typically induced by association of unfolded protein molecules via various chemical forces, namely disulfide linkages, electrostatic, hydrophobic interactions, and hydrogen bonds (Mulvihill and Kinsella, 1987;Oakenfull et al., 1997). Functional properties of heat-induced myofibrillar protein gel were mainly depended on chemical forces (Joseph et al., 1994;Wan et al., 1994). Previous literatures have showed the importance of chemical forces in heat-induced protein gels. Smyth et al. (1998) found that hardness of myosin gel could be weakened by adding dithiothreitol (DTT) to prevent the formation of disulfide bonds.Liu and Hsieh (2007) studied the molecular interactions of protein gels by adding DTT, urea and other reagents, and they concluded that non-covalent bonds played a more important role than disulfide bonds in the formation of heat-induced protein gels. Hermansson (1979) found that when less net electric charge were distributed on the surface of protein molecules, the electrostatic repulsion, hydrophobic attractions and intermolecular hydrogen bonds could keep a better balance, which made it easier to form ordered gel network. Hayakawa and Nakai (1985) reported that hydrophobic interactions of myosin were proposed to be the prerequisites for the formation of large aggregates. However, up to now, available data on chemical forces and the relationships between chemical forces and functional properties of MP gel are limited.Raman spectroscopy could be employed to investigate the chemical forces of heat-induced protein gel (Ikeda and Li-Chan, 2004;Li-Chan, 1996;Liu et al., 2011). Tryptophan (Trp) was a hydrophobic amino acid with hydrophobic residues. The normalized intensity of the Raman band near 760 cm −1 was assigned to the stretching vibration of the tryptophan residues ring and could be used to investigate the hydrophobicity of the Trpresidues, and then reflect the hydrophobic interactions of protein gel (Ikeda and Li-Chan, 2004;Li-Chan, 1996;Tu, 1982 -Chan, 2004;Li-Chan, 1996). Zeta potential presents the potential difference between the dispersion medium and the stationary layer of fluid attached to the dispersed particle and can be used to indicate the degree of electrostatic interactions between adjacent, similarly charged particles in a dispersion (Runkana et al., 2004).Several studies had been performed to investigate the effects of ionic strength on functional properties such as G', hardness and WHC (Bjorg et al, 1986;Boyer et al., 1996;Laure et al., 2014;Stone and Stanley, 1994 Materials and MethodsMaterials Six week-old commercial broilers (AA type) were purchased from a commercial chicken farm in Nanjing, China.Bovine serum albumin (BSA) was obtained from Sinopharm Chemical Reagent Co., Ltd (Shanghai, China). All chemicals used were of analytical grade. Methods Extraction of myofibrillar protein ...

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Section: Resultsmentioning

confidence: 99%

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

Zhang

Yang

Tang

et al. 2015

FSTR

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“…Dynamic rheology is very useful to determine protein functionality in meat processing, which contributes to gelation and is the basis for the development of texture (Cao, Xia, Zhou, & Xu, 2012;Hamann & MacDonald, 1992). The typical storage modulus (G′) and loss modulus (G″) of normal and PSE-like meat batters during heating from 25°C to 80°C were presented in Figure 2.…”

Section: Dynamic Rheological Measurementmentioning

confidence: 99%

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

Li¹,

Chen²,

Zhao³

et al. 2014

CyTA - Journal of Food

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The objective of this study was to evaluate the differences between normal and pale, soft, exudative (PSE)-like chicken breast meat in the chemical composition, pH, color, water binding capacity, textural properties, salt-soluble protein (SSP) extraction as well as dynamic rheological properties. Compared with normal meat, PSE-like chicken meat showed similar moisture, fat, and ash content (P > 0.05), but significantly lower protein content (P < 0.05). It had a significantly higher L* and lower pH and SSP extraction (P < 0.05). Heated PSE-like meat batter had lower water-binding capacity, textural characteristics (P < 0.05) and reduced gel elasticity (G′) and viscosity. However, the color variation of PSE-like meat gels was decreased. No significant changes were observed in the SSP electrophoretic patterns by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). In conclusion, PSE-like poultry meat changed the chemical composition and impaired protein functionality; however, the difference in color was small when used in further products.Keywords: PSE-like; chicken; gel properties; salt-soluble protein; dynamic rheology El objetivo del presente estudio se dirigió a evaluar las diferencias existentes entre la carne de pechuga de pollo normal y la de tipo PSE en términos de su composición química, pH, color, capacidad de retención de agua, propiedades texturales, extracción de proteína soluble en sal (PSS), así como sus propiedades reológicas dinámicas. En comparación con la carne de pollo normal, se constató que la carne de pollo tipo PSE exhibe un contenido de humedad, de grasa y de ceniza similar (P > 0,05), mientras que su contenido de proteína es significativamente inferior (P < 0,05). Asimismo, se observó que la carne tipo PSE tiene un nivel de L* más elevado, en tanto su pH y su extracción SSP son inferiores (P < 0,05). Al ser calentada, la masa de carne tipo PSE acusa niveles inferiores de capacidad de retención de agua, de características texturales (P < 0,05), reduciéndose, al mismo tiempo, la elasticidad de gel (G′) y la viscosidad. Sin embargo, en los geles de carne tipo PSE se constató la disminución de la variación de color. Frente a la aplicación de la SDS-PAGE, no se observaron cambios significativos en los patrones electroforéticos en la PSS. Se concluye que la composición química de la carne de pollo tipo PSE se ve alterada, lo cual limita su funcionalidad proteica. Sin embargo, la diferencia de color es reducida si se utiliza en productos posteriores.

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“…In the last decade, the food industry has shown a rising interest in high-pressure technologies as nonthermal processes to achieve food safety and improve or maintain the quality of some products [3,8,33]. However, HHP can affect protein conformation, change its functionality, and generate pressure transitions such as denaturation, aggregation, or gelation, which depend on pressure level, temperature, type of protein, and time [28].…”

Section: Introductionmentioning

confidence: 99%

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

et al. 2015

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The aim of this study was to evaluate the effect of HHP and rigor state on palm ruff (Seriolella violacea) muscle proteins. HHP treatments were performed at 450-550 MPa for 3 and 4 min at 15°C. Protein secondary structure was evaluated by using Fourier transform infrared spectroscopy, and the thermal behavior was evaluated by using differential scanning calorimetry. The results showed that HHP treatments reduced a-helix and increased b-sheet in fish protein structures. Throughout the 35-d storage period, secondary structures in HHP samples changed depending on pressure intensity, holding time, and rigor state. The thermograms of palm ruff muscles showed four endothermic transitions in prerigor state and three in postrigor state. The HHP treatment affected thermal stability of myosin protein, which is reflected in the change of denaturation temperature (T d ) and a decrease in denaturation enthalpy (DH d ) with respect to the native protein; actin was denatured by the pressure treatments. In conclusion, rigor state and HHP affected protein structure of fish proteins.

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The mechanism of high pressure-induced gels of rabbit myosin

Cited by 137 publications

References 42 publications

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

Effects of Ionic Strength on Chemical Forces and Functional Properties of Heat-induced Myofibrillar Protein Gel

A comparative study of chemical composition, color, and thermal gelling properties of normal and PSE-like chicken breast meat

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

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