Survival of Salmonella anatum Heated in Various Media

Survival of Salmonella anatum heated at 55 C for 35 min was determined in solutions of various chemical constituents of foods including salts, carbohydrates, amino acids, peptides, nucleic acids, gums, and stabilizers and compared with survival in 0.1 m phosphate buffer (pH 7.0). Commercially sterilized whole milk gave the most protection against heat. Trypticase Soy Broth, various peptide mixtures, and some amino acids gave substantial protection. Results with carbohydrates were variable, with mannitol, sucrose, and rhamnose providing substantial protection and glucose decreasing heat resistance. A few other substances, cysteine, glutathione, and sodium citrate, also decreased heat resistance. Pure proteins had little effect. Results show that water activity is of little significance under the test conditions. Protection from heat probably results from complexing of substances with heat-sensitive proteins in the cells. Autoclaved milk should not be considered equivalent to raw milk for studies of survival of bacteria during heating.     

Altered Mitochondrial Respiration in a Chromosomal Mutant of Neurospora crassa

A mutant of Neurospora crassa (cni-1) has been isolated that has two pathways of mitochondrial respiration. One pathway is sensitive to cyanide and antimycin A, the other is sensitive only to salicyl hydroxamic acid. Respiration can proceed through either pathway and both pathways together in this mutant account for greater than 90% of all mitochondrial respiration. The cni-1 mutation segregates as a nuclear gene in crosses to other strains of Neurospora. Absorption spectra of isolated mitochondria from cni-1 show typical b- and c-type cytochromes but the absorption peaks corresponding to cytochrome aa(3) are not detectable. Extraction of soluble cytochrome c-546 from these mitochondria followed by reduction with ascorbate reveals a new absorption peak at 426 nm that is not present in wild-type mitochondria. This peak may be due to an altered cytochrome oxidase with abnormal spectral properties. Mitochondria from cni-1 have elevated levels of succinate-cytochrome c reductase but reduced levels of nicotinamide adenine dinucleotide reduced form cytochrome c reductase and of cyanide- and azide-sensitive cytochrome c oxidase. These studies suggest that the cni-1 mutation results in the abnormal assembly of cytochrome c oxidase so that the typical cytochrome aa(3) spectrum is lost and the enzyme activity is reduced. As a consequence of this alteration, a cyanide-insensitive respiratory pathway is elaborated by these mitochondria which may serve to stimulate adenosine 5'-triphosphate production via substrate level phosphorylation by glycolysis and the Krebs cycle.