Enzymatic interesterification of anhydrous milk fat with rapeseed and/or linseed oil: oxidative stability

in Journal of Agricultural and Food Chemistry (2009), 57(15), 6787-6794

Blends of anhydrous milkfat (AMF) and linseed oil (70/30), and AMF, rapeseed oil (RO) and linseed oil (LO), 70/20/10, were submitted to enzymatic interesterification. The oxidative stability of the blends ... [more ▼]

Blends of anhydrous milkfat (AMF) and linseed oil (70/30), and AMF, rapeseed oil (RO) and linseed oil (LO), 70/20/10, were submitted to enzymatic interesterification. The oxidative stability of the blends, the interesterified (IE) blends and IE blends with 50 ppm -tocopherol added as antioxidant were studied. Samples were stored in open flasks at 60°C, 25°C and 4°C, and periodically submitted to peroxide, p-anisidine, TBA value determination and UV measurement at 232 and 268 nm. The analysis of volatile compounds was carried out by SPME for the samples stored at 60°C. Peroxides appeared to be the only significant oxidation products after 12 weeks storage at 4°C. As expected, the binary blends (BB) were more sensitive to oxidation than the ternary blends (TB). The BB were associated with increased volatile emission compared to TB. Interesterification led to variable effects on the oxidation of fat mixtures, depending on composition and temperature (beneficial effect on BB, at both 25°C and 60°C, and a rather neutral effect on TB). The IE blends exhibited higher volatile release prior to ageing. A pro-oxidant effect of -tocopherol addition was observed at 25°C on both BB and TB. At 60°C, an antioxidant effect was observed on TB. [less ▲]

Interesterification of rapeseed oil with anhydrous milk fat and its stearin fraction. II. Modifications of melting properties

in Groupement Consultatif International de Recherche sur le Colza (2009), 25

Chemical and/or physical modification of oils and fats are commonly used by food industry to widen their range of applications (1,2). Lipase-catalysed interesterification of anhydrous milk fat (AMF) and ... [more ▼]

Chemical and/or physical modification of oils and fats are commonly used by food industry to widen their range of applications (1,2). Lipase-catalysed interesterification of anhydrous milk fat (AMF) and various vegetable oils is now a well documented procedure (3-7). The purpose of this technique is to produce original structured fats with properties different from a simple blending, that may be used as spreads or introduced into pastry. The new fats contain higher amounts of polyunsaturated fatty acids (PUFA) than butter, which provides health benefits (8,9). To our knowledge only a few authors associated AMF fractionation with blending and interesterification (10,11), although this combination may be used to increase the ratio of vegetable oil in blends and thus the PUFA content of the product. The compositional changes occurring during the lipase-catalysed interesterification of AMF/rapeseed oil (RO) and AMF stearin fraction (AMFSF)/RO blends were described in the first part of this study. In the present and second part are reported the resulting changes in physical properties, especially the melting behaviour through solid fat content (SFC), dropping point (DP) and fusion profiles by differential scanning calorimetry (DSC). [less ▲]

Functional analysis of the cell division protein FtsW of Escherichia coli

in Journal of Bacteriology (2004), 186(24), 8370-8379

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in ... [more ▼]

Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation. This essential cell division protein has 10 transmembrane segments (TMSs). It is a late recruit to the division site and is required for subsequent recruitment of penicillin-binding protein 3 (PBP3) catalyzing peptide cross-linking. The results allow identification of several domains of the protein with distinct functions. The localization of PBP3 to the septum was found to be dependent on the periplasmic loop located between TMSs 9 and 10. The E240-A249 amphiphilic peptide in the periplasmic loop between TMSs 7 and 8 appears to be a key element in the functioning of FtsW in the septal peptidoglycan assembly machineries. The intracellular loop (containing the R166-FI78 amphiphilic peptide) between TMSs 4 and 5 and Gly 311 in TMS 8 are important components of the amino acid sequence-folding information. [less ▲]