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A set of 27 rice varieties were evaluated for their morphological grain characteristics (length, width, thickness, thousand kernel weight, TKW), chemical composition (amylose, protein, and ash content) and starch properties (gelatinization temperature and enthalpy, amylose-lipid complex). In addition, cell walls were characterized by the arabinoxylan and beta-glucan contents. A rapid method for determining optimum rice cooking time was developed based on the swelling ratio; a fixed value of 2.55 gave a gelatinization level of 95% assessed by differential scanning calorimetry and translucence testing. Optimum cooking time appears positively correlated with kernel thickness and TKW but also with ash content. Confocal laser and scanning electron microscope observation of uncooked rice grains revealed different structural features (cell size) and fracture behavior: for some cultivars, the fracture showed ruptured cells, whereas for others most cells were intact. These structural differences, which may be linked to pectin content, could partly explain rice kernel cooking behavior.

BackgroundPrevious research programmes have described muscle biochemical traits and gene expression levels associated with beef tenderness. One of our results concerning the DNAJA1 gene (an Hsp40) was patented. This study aims to confirm the relationships previously identified between two gene families (heat shock proteins and energy metabolism) and beef quality.ResultsWe developed an Agilent chip with specific probes for bovine muscular genes. More than 3000 genes involved in muscle biology or meat quality were selected from genetic, proteomic or transcriptomic studies, or from scientific publications. As far as possible, several probes were used for each gene (e.g. 17 probes for DNAJA1). RNA from Longissimus thoracis muscle samples was hybridised on the chips. Muscles samples were from four groups of Charolais cattle: two groups of young bulls and two groups of steers slaughtered in two different years. Principal component analysis, simple correlation of gene expression levels with tenderness scores, and then multiple regression analysis provided the means to detect the genes within two families (heat shock proteins and energy metabolism) which were the most associated with beef tenderness. For the 25 Charolais young bulls slaughtered in year 1, expression levels of DNAJA1 and other genes of the HSP family were related to the initial or overall beef tenderness. Similarly, expression levels of genes involved in fat or energy metabolism were related with the initial or overall beef tenderness but in the year 1 and year 2 groups of young bulls only. Generally, the genes individually correlated with tenderness are not consistent across genders and years indicating the strong influence of rearing conditions on muscle characteristics related to beef quality. However, a group of HSP genes, which explained about 40% of the variability in tenderness in the group of 25 young bulls slaughtered in year 1 (considered as the reference group), was validated in the groups of 30 Charolais young bulls slaughtered in year 2, and in the 21 Charolais steers slaughtered in year 1, but not in the group of 19 steers slaughtered in year 2 which differ from the reference group by two factors (gender and year). When the first three groups of animals were analysed together, this subset of genes explained a 4-fold higher proportion of the variability in tenderness than muscle biochemical traits.ConclusionThis study underlined the relevance of the GENOTEND chip to identify markers of beef quality, mainly by confirming previous results and by detecting other genes of the heat shock family as potential markers of beef quality. However, it was not always possible to extrapolate the relevance of these markers to all animal groups which differ by several factors (such as gender or environmental conditions of production) from the initial population of reference in which these markers were identified.

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Hereditary breast cancers account for up to 5-10 % of breast cancers and a majority are related to the BRCA1 and BRCA2 genes. However, many families with breast cancer predisposition do not carry any known mutations for BRCA1 and BRCA2 genes. We explored the incidence of rare large rearrangements in the coding, noncoding and flanking regions of BRCA1/2 and in eight other candidate genes--CHEK2, BARD1, ATM, RAD50, RAD51, BRIP1, RAP80 and PALB2. A dedicated zoom-in CGH-array was applied to screen for rearrangements in 472 unrelated French individuals from breast-ovarian cancer families that were being followed in eight French oncogenetic laboratories. No new rearrangement was found neither in the genomic regions of BRCA1/2 nor in candidate genes, except for the CHEK2 and BARD1 genes. Three heterozygous deletions were detected in the 5' and 3' flanking regions of BRCA1. One large deletion introducing a frameshift was identified in the CHEK2 gene in two families and one heterozygous deletion was detected within an intron of BARD1. The study demonstrates the usefulness of CGH-array in routine genetic analysis and, aside from the CHEK2 rearrangements, indicates there is a very low incidence of large rearrangements in BRCA1/2 and in the other eight candidate genes in families already explored for BRCA1/2 mutations. Finally, next-generation sequencing should bring new information about point mutations in intronic and flanking regions and also medium size rearrangements.

The relationship between the content of N-acetylneuraminic acid residues of micellar -casein and acid coagulability of milk was investigated. At 30 °C, partial deglycosylation of micellar -casein does not significantly affect the content of micellar proteins, micellar surface charge, and micellar solvation. Casein micelles modified by the release of part of the N-acetylneuraminic acid residues showed a shorter acid gelation time, a higher rate of gel strengthening, and a higher final firmness. This enhancement in the gelation ability of the neuraminidase-treated casein micelles of milk should appear as the result of increase in number of hydrophobic sites on the surface of casein micelle due to enzymatic deglycosylation of micellar -casein.

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