Formation of tetracycline degradation products in chicken and pig meat under different thermal processing conditions.

Tetracycline (TC) and 4-epitetracycline (4eTC) degradation, as well as anhydrotetracycline (ATC) and 4-epianhydrotetracycline (4eATC) formation, has been evaluated in thermally treated chicken breast, pig loin, and pig loin with added back-fat. Samples containing TC and 4eTC residues were submitted to microwave or boiling heating, extracted with a mixture of McIlvaine buffer/methanol (75:25), and analyzed by high-performance liquid chromatography-diode array detection on a phenyl-hexyl reverse phase chromatographic column. The formation of ATC and 4eATC, as well as of two unidentified compounds, was described for the first time in edible meat samples submitted to mild thermal treatments, similar to those applied at home to cook foods.

Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions.

Application of high pressure can be used for gentle pasteurizing of food, minimizing undesirable alterations such as vitamin losses and changes in taste and color. In addition, pressure has become a useful tool for investigating structural changes in proteins. Treatments of proteins with high pressure can reveal conformations that are not obtainable by other physical variables like temperature, since pressure favors structural transitions accompanied with smaller volumes.

Dual nature of the infectious prion protein revealed by high pressure.

Crude brain homogenates of terminally diseased hamsters infected with the 263K strain of scrapie (PrP(Sc)) and purified prion fibrils were heated or pressurized at 800 megapascals and 60 degrees C for 2 h in different buffers and in water. Prion proteins (PrP) were analyzed for their proteinase K resistance in immunoblots and for their infectivity in hamster bioassays. A notable decrease in the proteinase K resistance of unpurified prion proteins, probably because of pressure-induced changes in the protein conformation of native PrP(Sc) or the N-truncated PrP-(27-30), could be demonstrated when pressurized at initially neutral conditions in several buffers and in water but not in a slightly acidic pH.

Reduced proteinase K resistance and infectivity of prions after pressure treatment at 60 degrees C.

High hydrostatic pressure is a mild technology compared with high temperatures and is commonly used for food pasteurization. Crude brain homogenates of terminally diseased hamsters infected with scrapie 263K strain were heated at 60 degrees C and/or pressurized up to 1000 MPa for 2 h. Prion proteins were analysed for their proteinase K sensitivity using a Western blot technique.

Pressure/temperature combined treatments of precursors yield hormone-like peptides with pyroglutamate at the N terminus.

Peptides containing the cyclic product of glutamine at the N terminus are usually biologically active. If the cyclization of glutamine was associated with a volume reduction, pressure should displace the equilibrium in the direction of the lower volume. Here, results in model solutions and in whey are discussed, showing that the theorized cyclization of glutamine in Gln-His-ProNH(2) or Gln-Leu-ProNH(2) is significantly accelerated during the application of heat and even more strongly when elevated temperature and pressure combinations are used.

Mechanism-based irreversible inactivation of horseradish peroxidase at 500 MPa.

The effects of high-pressure treatment on the reaction rates of horseradish peroxidase (HRP) with guaethol or guaiacol as a hydrogen donor were evaluated from direct transmission measurements in a high-pressure optical cell at 435 nm. Peroxidases are known to be very barostable and insensitive to heat. With guaethol the reaction velocity was independent of pressure up to 500 MPa, but with guaiacol the cytochrome c oxidase underwent a mechanism-based irreversible inhibition of catalytic activity when subjected to pressure; in the resting states (fully oxidized or reduced), it was insensitive to pressure.