Raman spectroscopy study of the structural effect of microbial transglutaminase on meat systems and its relationship with textural characteristics

Herrero, Ana M.; Cambero, M.I.; Ordóñez, J.A.; Hoz, Lorenzo de la; Carmona, Pedro

doi:10.1016/j.foodchem.2007.12.003

Cited by 130 publications

(80 citation statements)

References 23 publications

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“…The water spectrum was previously subtracted from the spectra by following the criteria as described in the literature (Alix et al, 1988;Herrero et al, 2008).…”

Section: Sulfhydryl Group Content Measurementmentioning

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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“…The water spectrum was previously subtracted from the spectra by following the criteria as described in the literature (Alix et al, 1988;Herrero et al, 2008).…”

Section: Sulfhydryl Group Content Measurementmentioning

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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“…1 shows typical Raman spectra of unheated and heated meat batters without and with soy protein (3% and 6%) in the 800-1725 cm À1 region. The Raman bands were assigned according to the literature (Li-Chan, 1996;Herrero et al, 2008a). Secondary and tertiary protein structural changes and water structural modifications were determined from modifications in frequency and intensity of the Raman bands.…”

Section: Texture Profile Analysismentioning

confidence: 99%

“…Structural studies of thermal gelation of meat and fish products have also been performed using this technique (Bouraoui, Nakai, & Li-Chan, 1997;Sánchez-González et al, 2008;Herrero, Carmona, López-López, & Jiménez-Colmenero, 2008b). Recently, Raman spectroscopic studies have also been conducted to examine the structural changes that occur in meat proteins upon addition of cold-set binding agents to meat systems (Herrero, Cambero, Ordóñez, de la Hoz, & Carmona, 2008a). This technique has also been used to study the structure of various non-meat proteins such as egg albumen, whey and plasma proteins during the formation of heat-induced gels (AlizadehPasdar, Nakai, & Li-Chan, 2002;Ikeda, 2003;Ngarize, Adams, & Howell, 2005;Dávila, Páres, & Howell, 2006;Dávila, Páres, & Howell, 2007).…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment

Herrero

Carmona

Cofrades

et al. 2008

Food Research International

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a b s t r a c tThis article reports an assessment of the potential of Raman spectroscopy for determination of structural changes in meat batter with and without soy protein isolate (SPI) upon heating. It also reports proximate composition, water binding and texture analyses. Various meat batters were made up for this purpose: a control meat batter and meat batters with 3% and 6% SPI with and without thermal treatment (70°C/ 30 min). Results showed an increase (P < 0.05) in penetration force, hardness and chewiness upon heating. In heated samples, increases (P < 0.05) in hardness and chewiness were observed as a result of SPI addition. Just in heated meat batter with added SPI, Raman spectroscopy analysis revealed decrease (P < 0.05) in a-helix accompanied by an increase (P < 0.05) in b-sheet structures after heating. Significant correlations were found between these secondary structural changes in meat proteins and water binding and textural properties of the meat batters.

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“…Although, small meat pieces can also be restructured into larger pieces using NaCl and sodium tripolyphosphate, this can lead to flavour changes that are not desirable, as well as increasing sodium intake (Kuraishi et al, 2000;Muguruma et al, 2003). In recent studies with Raman spectroscopy, TGase was observed to cause a significant decrease in a-helix content and a significant increase in b-sheets in meat proteins (Herrero, Cambero, Ordóñez, de la Hozand, & Carmona, 2008). Therefore, treatment with TGase would be expected to affect the ability of proteins to aggregate (Fernandez-Diaz, Montero, & Gomez-Guillen, 2001;Herrero et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…In recent studies with Raman spectroscopy, TGase was observed to cause a significant decrease in a-helix content and a significant increase in b-sheets in meat proteins (Herrero, Cambero, Ordóñez, de la Hozand, & Carmona, 2008). Therefore, treatment with TGase would be expected to affect the ability of proteins to aggregate (Fernandez-Diaz, Montero, & Gomez-Guillen, 2001;Herrero et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Dielectric properties of chicken and fish muscle treated with microbial transglutaminase

2010

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Raman spectroscopy study of the structural effect of microbial transglutaminase on meat systems and its relationship with textural characteristics

Cited by 130 publications

References 23 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

Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment

Dielectric properties of chicken and fish muscle treated with microbial transglutaminase

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