Seventeen propanolamines, six diisopropanolamines, and two butanolamines were studied for their antimicrobial properties against a mixed flora of fungi and bacteria in cutting fluids. All of the propanolamines showed inhibitory properties in the lubricants. Isopropanolamines were found to have very weak antimicrobial properties, and both butanolamine compounds were inhibitory. The most active compound found was L-2-methylamino-1-phenolpropanol, but other chemicals including DL-2-benzylamino-1-propanol, 3-diethylamino-1-propanol, 2-amino-2-methyl-1-propanol, 2-dimethylamino-2-methyl-1-propanol, 1-dimethylamino-3-propanol, and 3-amino-1-propanol all showed good antimicrobial properties in the products.
The attaching ability of a number of bacteria, isolated from bovine rumen and animal intestine, to starch granules was examined in vitro. Among bacteria examined in the present investigation, strains possessing the attaching ability to starch were those belonging to an untypable Bacteroides sp., Bacteroides amylophilus, Bacteroides oralis, Bacteroidesruminicola ss. ruminicola, an untypable Bifidobacterium sp., Bifidobacteriumthermophilum, Bifidobacterium pseudolongum, and Bifidobacteriumlongum. The reaction temperature had a profound effect on the attachment of bacteria to starch. All of bacteria listed above attached well to starch at 38°. Strains of the untypable Bacteroides sp., B. oralis, B. thermophilum, B. pseudolongum, and B. longum attached to starch even at the reaction temperature of 4°. On the other hand, those of B. amylophilus did not attach to starch at 4°. The activity of several hydrolases of various kinds of bacteria was examined. The amylase activity of cells of bacteria capable of attaching to starch was remarkably high, compared with that of bacteria incapable of attaching. Bacteria such as B. fibrisolvens and Streptococcus bovis, which were incapable of attaching to starch but possessed intense amylolytic activity, secreted extracellularly large parts of amylase produced by them. Only Peptostreptococcus productus among examined bacteria exhibited remarkably intense urease activity. There was no significant difference in the specific activity of the remaining three hydrolases between bacteria capable and incapable of attaching to starch. The attachment of bacteria to starch was inhibited by various carbohydrates. Carbohydrates like dextrin, amylose, amylopectin, soluble starch, and derivatives of starch except carboxymethyl-starch inhibited the attachment of bacteria to starch. The degree of this inhibition by these carbohydrates depended on their concentrations. Other carbohydrates examined, including derivatives of cellulose and dextran, did not inhibit significantly the attachment of bacteria to starch. An attempt was made to detach or elute bacteria from starch by some means. Cells of B. amylophilus, once attached to starch at 38°, were detached by the cooling treatment at 4°. Although both cells of B. thermophilum and B. pseudolongum were not detached from starch by the cooling treatment at 4°, they were eluted from starch with a solution of dextrin or partially-hydrolysed hydroxypropyl-starch. Cells of Bacteroides sp. 7-4, once attached to starch, were not detached either by the cooling treatment at 4° or by the elution treatment with a solution of above two carbohydrates.
Flavobacterium devorans ATCC 10829 (=NRRL B-54=KM 1367) was compared with Pseudomonas paucimobilis NCTC 11030 (type, =KM 2395), 11031 (=KM 2396), and 11032 (=KM 2397) in respect to more than 65 phenotypic tests, susceptibility to 15 antimicrobial agents, electron-microscopy, and visible absorption spectrum of yellow pigments in acetone extracts of bacterial cells. Long-chain base component of ceramide glucuronic acid in cellular lipids was quantitatively determined from thin-layer chromatogram of hexane-ether extract from the hydrolysate of acetone-dried cells of 4 strains. Characteristic profile of cellular fatty acids of strain 10829, as well as of 3 P. paucimobilis strains, was the presence of 2-hydroxymyristic acid, palmitic acid, and octadecenoic acid in high concentration. Because of the phenotypic and analytical similarities and high percentage of guanine plus cytosine content in deoxyribonucleic acid, F. devorans 10829 was reidentified as a strain of P. paucimobilis. Since the strain ATCC 10829 was a misidentified organism, the name Flavobacterium devorans can not be a senior synonym over Pseudomonas paucimobilis. Unless the authentic strain of the original describer of F. devorans or any isolate in conformity with the original description for the species were found, the name Flavobacteriumdevorans should not be retained further.
The density of membrane-associated particles (MAPs) was examined by freeze-fracture technique on Escherichia coli cells grown aerobically with or without glucose. The MAP density of the cells grown with glucose was about 1/2 compared with that of the cells grown without glucose. In parallel with this decrease of the MAP density, the amount of cytochrome b1 and succinate dehydrogenase activity were also reduced in the cells grown with glucose. By the addition of inorganic phosphate, however, the MAP density and cytochrome b1 content increased simultaneously in the cells grown with glucose, although activity of succinate dehydrogenase did not increase.
Acid digests and enzyme digests (trypsin and pepsin) prepared from rapeseed oil meal were evaluated for use as nitrogenous ingredients in microbiological media. Acid and trypsin digests compared favourably with commercial media in supporting the growth of Candida utilis. The results demonstrate a novel use for rapeseed oil meal, independent of the inherent problems in utilization of this product, namely, toxicity, palatability, and digestibility.
Urease and extracellular DNase activities were tested in 292 strains belonging to 125 species of 33 genera. Basidiomycetous yeasts and related species had both urease and extracellular DNase. Species belonging to the genera Rhodotorula and Cryptococcus, and four species of Candida (Candida curvata, Candida humicola, Candida bogoriensis, and Candida diffluens) which are considered to be closely related to basidiomycetous yeasts, showed both activities. In general, ascosporogenous yeasts and their imperfect forms did not have either urease or extracellular DNase. Hansenula bimundalis and Saccharomycopsis lipolytica showed both enzymes, but the activities were weaker than those of basidiomycetous yeasts. Schizosaccharomyces pombe, Schizosaccharomycesoctosporus, Citeromyces matritensis, Lipomyces starkeyi, and Nadsonia elongata had urease but not extracellular DNase. Saccharomycopsisfibuligera, Hansenula jadinii, Hansenula minuta, Pichia pinus, Pichia rhodanensis, and Candida pseudotropicalis showed extracellular DNase but not urease. Taxonomic significance of urease and extracellular DNase is discussed.
The steady-state extensional growth rate of five unknown (un, TS) mutants of Neurospora crassa at various temperatures was measured. Data from Dr. R. K. Littlewood on growth of two extrachromosomal mutants are presented for comparison. The optimum growth temperature of six of the seven mutants is 5-10° lower than that of wild-type. The free energies of inactivation of the mutants are significantly greater than that of wild type. Six of the seven also exhibit relatively large energies of activation. Thus, all of the mutants are "hot" sensitive and six of the seven are also cold sensitive. All of the TS mutants are osmotically remedial at either high or low temperatures or both. Biochemical data indicate that at least some nutritionally irreparable, temperature-extremity sensitive, osmotically remedial mutants may be defective in cell wall or membranes; however, there are reasons to believe that this phenotype is not unique to such lesions.
Edited and published by : Applied Microbiology, Molecular and Cellular Biosciences Research Foundation/Center for Academic Publications Japan Produced and listed by : TERRAPUB, Center for Academic Publications Japan/Shobi Printing Co., Ltd. (-Vol.60,No12), Center for Academic Publications Japan/InternationalAcademic Printing Co., Ltd.(-Vol.54,No1)