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Brevibacterium linen

Dufosse, L. and de Echanove, C., The last step in the biosynthesis of aryl carotenoids in the cheese ripening bacteria Brevibacterium linens ATCC 9175 (Brevibacterium aurantiacum sp. nov.) involves a cytochrome P450-dependent monooxygenase. Food Res. Int, 38, 967, 2005. [Pg.426]

Guyomarc h, R, Binet, A., and Dufosse, L., Characterization of Brevibacterium linens pigmentation using spectrocolorimetry, Int. J. Food Microbiol., 57, 201, 2000. [Pg.426]

Scheme 23.22 Some nitrogen-containing flavour compounds produced by microorganisms, a Methylanthranilate formation from N-methyl methylanthranilate 1 Trametes sp., Polyporus sp. b Different pyrazines produced with microorganisms in optimised media 2 mutant strain from Pseudomonas perolens ATCC 10757 3 Bacillus subtilis, Brevibacterium linens 4 mutant strain of Corynebacterium glutamicum... Scheme 23.22 Some nitrogen-containing flavour compounds produced by microorganisms, a Methylanthranilate formation from N-methyl methylanthranilate 1 Trametes sp., Polyporus sp. b Different pyrazines produced with microorganisms in optimised media 2 mutant strain from Pseudomonas perolens ATCC 10757 3 Bacillus subtilis, Brevibacterium linens 4 mutant strain of Corynebacterium glutamicum...
In surface smear-ripened cheeses, e.g. Munster, Limburger, Tilsit, Trapist, the surface of the cheese is colonized first by yeasts which catabolize lactic acid, causing the pH to increase, and then by Brevibacterium linens, the characteristic micro-organism of the surface smear but which does not grow below pH 5.8, and various other micro-organisms, including Micrococcus, Arthrobacter and coryneform bacteria. [Pg.326]

Production of antibiotic-like substances in cultured dairy products has been associated with homo- and heterolactic streptococci, some of the lactobacilli, and Brevibacterium linens. Production may be unwanted and fortuitous, as in commercial starter cultures, or it may be desired and encouraged. [Pg.694]

Beattie, S. E. and Torrey, G. S. 1984. Volatile compounds produced by Brevibacterium linens inhibit mold spore germination (abstract). J. Dairy Sci. 67 (suppl. 1), 84. Berry, E. C. and Bullerman, L. B. 1966. Use of cheese whey for vitamin Bi2 production. [Pg.720]

Foissy, H. 1974. Examination of Brevibacterium linens by an electrophoretic zymogram technique. J. Gen. Microbiol 80, 197-207. [Pg.723]

Foissy, H. 1978A. Aminopeptidase from Brevibacterium linens Production and purification. Milchwissenschaft 33, 221-223. [Pg.723]

Foissy, H. 1978B. Some properties of aminopeptidase from Brevibacterium linens. FEMS Microbiol. Lett. 3, 207-210. [Pg.723]

Foissy, H. 1978C. Aminopeptidase from Brevibacterium linens Activation and inhibition. Z. Lebensm. Unters.-Forsch. 166, 164-166. [Pg.723]

Grecz, N., Wagenaar, R. O. and Dack, G. M. 1959. Inhibition of Clostridium botulinum by culture filtrates of Brevibacterium linens. J. Bacteriol. 78, 506-510. [Pg.725]

MGL catalyzes the o ,7-elimination reaction of methionine to a-ketobutyrate, methanethiol, and ammonia. MGL has been isolated from a number of bacteria, including Pseudomonas putida, Aeromonas sp., Clostridium sporogenes, P. taetrolens, and Brevibacterium linens, from the primitive protozoa Entamoeba histolytica and Trichomonas vaginalis, but is not believed to be present in yeast, plants, or mammals. " " Two MGL isoforms have been isolated from T. vaginali and Entamoeba histolytica, which differ in substrate specificity, overall charge, and catalytic properties. They show a high degree of sequence identity to MGL from Pseudomonas putida. MGL has demonstrated antitumor efficacy in a number of methionine-dependent cancer cell lines. ... [Pg.308]

Brevibacterium linens, a characteristic component of the surface microflora of smear-ripened varieties, has a strong proteolytic activity (Gripon et al, 1991). The extracellular proteinases secreted by a number of Br. linens strains have been partially purified (see Rattray et al, 1995). The proteinase secreted by Br. linens ATCC 9174 was purified to homogeneity by Rattray et al (1995) and found to be a serine proteinase with optimum activity at pH 8.5 and 50°C. It appears to be a trimeric enzyme with a monomeric mass of 56 kDa. The sequence of the 20 N-terminal amino acids showed no homology with the published sequences of other bacterial proteinases (Rattray 1995). Foissy (1974) reported on both intra- and extracellular proteinases but they were not studied further an extracellular aminopeptidase was purified by Foissy (1978). Sprhaug (1981) described a number of peptidase activities in cell-free extracts of Br. linens. [Pg.224]

Rattray, F. P., Fox, P. F., and Bockelmann, W. (1995). Purification and characterization of an extracellular proteinase from Brevibacterium linens ATCC 9174. Appl. Environ. Microbiol. 61, 3454-3456. [Pg.319]

Sprhaug, T. (1981). Comparison of peptide hydrolases from six strains of Brevibacterium linens. Milchwissenschaft 36, 137-139. [Pg.322]

Sprhaug, T., and Ordal, Z. J. (1974). Cell-bound lipase and esterase of Brevibacterium linens. Appl. Microbiol. 27, 607-608. [Pg.322]

Nature did however not develop blue carotenoids by increasing the number of double bonds. The longest conjugated systems in natural carotenoids, as known so far, extends to 15 double bonds and corresponds to a red hue (Fig. 7.17). Examples are tetraterpenes such as 3,3 ,4,4 -tetrahydrolycopene (in unripe tomatoes) and 3,3 -dihydroxyisorenieratene (in Brevibacterium linens... [Pg.605]

Brevibacterium linens is ubiquitously present, and populates also the human skin, where it causes e.g. foot odour. It is contained in the reddish smear coat ofRemoudou and other Belgian cheeses. The oxidation of its red pigment leads to a tremendous bathochromic shift (about 100 nm). [Pg.607]

Red smear cheese (e.g., Esrum, Munster) Same as for cheeses with small holes with a surface smear of Brevibacterium linens... [Pg.228]

To, B. C. S., Etzel, M. R. (1997b). Survival of Brevibacterium linens (ATCC 9174) after spray drying, freeze drying, or freezing. Journal of Food Science, 62(1), 167-189. [Pg.269]

Bacteriocin. Prod, by Brevibacterium linens M 18. Active against gram-positive bacteria. [Pg.265]


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See also in sourсe #XX -- [ Pg.228 ]

See also in sourсe #XX -- [ Pg.383 ]




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