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Bighead carp head soup is a traditional Chinese cuisine with a pleasant aroma, but the effect of fish head phospholipids (FPLs) on the odorants is not fully understood. In this study, nuclear magnetic resonance (NMR), attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) and headspace solid-phase microextraction gas chromatography–mass spectrometry (HS-SPME–GC–MS) were used to monitor the oxidation products of phospholipids in fish head soup during the cooking process, and the fish head triglycerides (FTGs) were used as controls. In 1H NMR spectra, the signals of unsaturated acyl groups and the oxidation compounds in FPLs were significantly higher than those in FTGs. The results of FTIR showed that the changes of functional group absorptions of the oxidation compounds in FPLs were greater than FTGs. GC–MS demonstrated that FPLs samples produced more lipid-derived volatile compounds than FTGs samples. These results showed that FPLs were more prone to oxidation and could produce more lipid-derived odorants. Therefore, FPLs rather than FTGs, were the main precursor substance of lipid-derived odorants in bighead carp head soup. • NMR, ATR-FTIR and HS-SPME–GC–MS used to monitor phospholipid oxidation in fish head soup. • Unsaturated acyl groups and oxidation compounds in FPLs higher than those in FTGs. • FPLs samples produced more lipid-derived volatile compounds than FTGs samples. • FPLs were the main precursors of lipid-derived odorants in bighead carp head soup. [ABSTRACT FROM AUTHOR]

1-Acyl- sn -glycerol-3-phosphate O -acyltransferase (PlsC) plays an essential role in the formation of phosphatidic acid, a precursor of various membrane phospholipids (PLs), in bacteria by catalyzing the introduction of an acyl group into the sn -2 position of lysophosphatidic acid. Various bacteria produce more than one PlsC. However, the physiological significance of the occurrence of multiple PlsCs is poorly understood. A psychrotrophic bacterium, Shewanella livingstonensis Ac10, which produces eicosapentaenoic acid at low temperatures, has five putative PlsCs (PlsC1-5). We previously showed that PlsC1 is responsible for the production of PLs containing an eicosapentaenoyl group. Here, we characterized another putative PlsC of this bacterium named PlsC4. We generated a plsC4 -disrupted mutant and found that PLs containing 13:0 found in the parental strain were almost completely absent in the mutant. The loss of these PLs was suppressed by introduction of a plsC4 -expression plasmid. PLs containing 15:0 were also drastically decreased by plsC4 disruption. Gas chromatography-mass spectrometry analysis of fatty acyl methyl esters derived from PLs of the parental strain showed that the 13:0 and 15:0 groups were an 11-methyllauroyl group and a 13-methylmyristoyl group, respectively. Phospholipase A2 treatment revealed that these fatty acyl groups were linked to the sn -2 position of PLs. Thus, PlsC4 is a new type of PlsC homolog that is responsible for the synthesis of PLs containing a branched-chain fatty acyl group at the sn -2 position and plays a clearly different role from that of PlsC1 in vivo . [ABSTRACT FROM AUTHOR]

Abstract: The generality of acyl transfer from phospholipids to membrane-active peptides has been probed using liquid chromatography–mass spectrometry analysis of peptide–lipid mixtures. The peptides examined include melittin, magainin II, PGLa, LAK1, LAK3 and penetratin. Peptides were added to liposomes with membrane lipid compositions ranging from pure phosphatidylcholine (PC) to mixtures of PC with phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol. Experiments were typically conducted at pH7.4 at modest salt concentrations (90mM NaCl). In favorable cases, lipidated peptides were further characterized by tandem mass spectrometry methods to determine the sites of acylation. Melittin and magainin II were the most reactive peptides, with significant acyl transfer detected under all conditions and membrane compositions. Both peptides were lipidated at the N-terminus by transfer from PC, phosphatidylethanolamine, phosphatidylserine or phosphatidylglycerol, as well as at internal sites: lysine for melittin; serine and lysine for magainin II. Acyl transfer could be detected within 3h of melittin addition to negatively charged membranes. The other peptides were less reactive, but for each peptide, acylation was found to occur in at least one of the conditions examined. The data demonstrate that acyl transfer is a generic process for peptides bound to membranes composed of diacylglycerophospholipids. Phospholipid membranes cannot therefore be considered as chemically inert toward peptides and by extension proteins. [Copyright &y& Elsevier]