Ana M. Herrero

Raman spectroscopy for monitoring protein structure in muscle food systems.

Raman spectroscopy offers structural information about complex solid systems such as muscle food proteins. This spectroscopic technique is a powerful and a non-invasive method for the study of protein changes in secondary structure, mainly quantified, analysing the amide I (1650–1680 cm− 1) and amide III (1200–1300 cm− 1) regions and C-C stretching band (940 cm− 1), as well as modifications in protein local environments (tryptophan residues, tyrosil doublet, aliphatic aminoacids bands) of muscle food systems. Raman spectroscopy has been used to determine structural changes in isolated myofibrillar and connective tissue proteins by the addition of different compounds and by the effect of the conservation process such as freezing and frozen storage. It has been also shown that Raman spectroscopy is particularly useful for monitoring in situ protein structural changes in muscle food during frozen storage. Besides, the possibilities of using protein structural changes of intact muscle to predict the protein functional properties and the sensory attributes of muscle foods have been also investigated. In addition, the application of Raman spectroscopy to study changes in the protein structure during the elaboration of muscle food products has been demonstrated.

Breaking strength of dry fermented sausages and their correlation with texture profile analysis (TPA) and physico-chemical characteristics

In order to assess its usefulness for monitoring textural properties of dry fermented sausages (chorizo, salchichon, salami, fuet and mini-fuet) the determination of breaking strength (BS) was evaluated. Texture profile analysis (TPA) and physico-chemical measurements (pH, aw, dry matter, fat content) were also performed. The BS determined by tensile test and TPA analysis produced complementary information that allowed these meat products to be grouped according to four different textural profiles. These profiles were characterized (p<0.05) by the values of BS, hardness, adhesiveness, cohesiveness and springiness. Multivariate analysis confirmed that BS and TPA parameters were correlated significantly (p<0.00005). On basis of these results, TPA parameters could be used to construct regression models to predict BS and therefore, to obtain a more complete textural property description of the dry fermented sausages. The resulting regression model was BS=-0.777+0.728∗adhesiveness-16881∗cohesiveness+1884.61∗springiness+0.042∗hardness (R(2)=0.634, p<0.00005).

Tensile properties of cooked meat sausages and their correlation with texture profile analysis (TPA) parameters and physico-chemical characteristics

The possibilities of using breaking strength (BS) and energy to fracture (EF) for monitoring textural properties of some cooked meat sausages (chopped, mortadella and galantines) were studied. Texture profile analysis (TPA), folding test and physico-chemical measurements were also performed. Principal component analysis enabled these meat products to be grouped into three textural profiles which showed significant (p<0.05) differences mainly for BS, hardness, adhesiveness and cohesiveness. Multivariate analysis indicated that BS, EF and TPA parameters were correlated (p<0.05) for every individual meat product (chopped, mortadella and galantines) and all products together. On the basis of these results, TPA parameters could be used for constructing regression models to predict BS. The resulting regression model for all cooked meat products was BS=-0.160+6.600∗cohesiveness-1.255∗adhesiveness+0.048∗hardness-506.31∗springiness (R(2)=0.745, p<0.00005). Simple linear regression analysis showed significant coefficients of determination between BS (R(2)=0.586, p<0.0001) versus folding test grade (FG) and EF versus FG (R(2)=0.564, p<0.0001).

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

Raman spectroscopy and texture analysis (TPA) studies were carried out to determine the effect of adding different levels of microbial transglutaminase (MTGase) to meat systems. This addition produced a significant (p<0.05) increase in hardness, springiness and cohesiveness in the meat systems. Raman spectroscopy analysis revealed the occurrence of secondary structural changes in meat proteins due to MTGase. Modifications in the amide I (1650-1680cm(-1)) and amide III (1200-1300cm(-1)) regions indicated a significant (p<0.05) decrease in α-helix content, accompanied by a significant (p<0.05) increase in β-sheets and turns due to the addition of the enzyme to meat systems. Significant (p<0.05) correlations were found between these secondary structural changes in meat proteins and the textural properties (hardness, adhesiveness, springiness and cohesiveness) of meat systems.