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Pseudomonas fragi

Nashif, S. A. and Nelson, F. E. 1953B. The lipase of Pseudomonas fragi. II. Factors affecting lipase production. J. Dairy Sci. 36, 471-480. [Pg.732]

Noreau, J. and Drapeau, G. R. 1979. Isolation and properties of the protease from the wild-type and mutant strains of Pseudomonas fragi. J. BacterioL 140, 911-916. [Pg.732]

Porzio, M. A. and Peeirson, A. M. 1975. Isolation of an extracelluleir neutred proteinase from Pseudomonas fragi. Biochim. Biophys. Acta 384, 235-241. [Pg.733]

Pseudomonas fragi (enantioselective) Pseudomonas sp. lipase (enantioselective)... [Pg.1963]

C Vasseur, J Labadie, M Elebraud. Differential protein expression by Pseudomonas fragi submitted to various stresses. Electrophoresis 20 2204-2213, 1999. [Pg.592]

Buchert, J., Viikari, L., Linko, M. and Markkanen, P. 1986. Production of Xylonic Acid by Pseudomonas Fragi. Biotechnol. Lett., 8, 541-546. [Pg.94]

Buchert, J., Puls, J. andPoutanen, K. 1988. Comparison of Pseudomonas Fragi and Gluconobac-ter Oxydans for Production of Xylonic Acid from Hemicellulose Hydrolyzates. Appl. Microbiol. Biotechnol., 28, 367-372. [Pg.94]

Kugimiya, W., Otani, Y., Hashimoto, Y., Tagaki, Y. 1986. Molecular cloning and nucleotide sequence of the lipase gene from Pseudomonas fragi. Biochem. Biophys. Res. Commun. 141, 185-190. [Pg.545]

Lu, J.Y., Liska, B.J. 1969. Lipase from Pseudomonas fragi. Properties of the enzyme. Appl. Microbiol. 18, 108-113. [Pg.546]

Lactobacillus casei, L. diacetylactis, Pseudomonas fragi Ethyl butyrate Eruity... [Pg.146]

Hood, S.K. and Zottolla, E.A. 1997. Growth media and surface conditioning influence the adherence of Pseudomonas fragi, Salmonella typhimurium and Listeria monocytogenes cells to stainless steel. Journal of Food Protection 60 1034-1037. [Pg.161]

Minimal in motor activity of albino rats Growth minima Pseudomonas fragi, streptococcus faecalis. [Pg.200]

Endoproteinase Asp-N Origin Pseudomonas fragi (mutant) Roche Diagnostics Endoproteinase Asp-N, Sequencing Grade... [Pg.1510]

In the soil the active substance is broken down by the soil bacterium Pseudomonas fragi into N,N-dimethyl-/7-phenylene diamine. Like the original active substance, this decomposition product is toxic to Pythium app. (Karanth et al.,... [Pg.458]

Oleuropein and its aglycone inhibit Lactobacillus plantarum, Pseudomonas fragi, Staphylococcus camosus, Enterococcus faecali.s, Bacillus cereus, Salmonella enteritidis and, moreover, a serial of fungi [89], The phenolic compounds act on the exoprotein secretion of the Staphylococcus aureus too [90],... [Pg.896]

Stone, L.S. and Zottola, E.A., 1985, Relationship between the growth phase of Pseudomonas fragi and its attachment to stainless steel. J. Food Sci. 50, 957 - 960. [Pg.267]

By bacterial manipulation, what is meant is that certain bacteria are used to slow down corrosion. For example, it has been reported " that carbon steel corrosion in presence of the biofihn of aerobic bacterium Pseudomonas fragi or the facultative anaerobe Escherichia coli had been slowed down by 2-fold to 10-fold. Another example is a biofilm-producing baclerinm, identified as Bacillus sp., that was able to reduce corrosion rates of mild steel by establishment of antimicrobial agent-producing biofllm, which inhibited the activity of SRB. [Pg.95]

Some pH optima for lipases of microorganisms are Penicillium chryso-genum, 6.2-6.S (277), Pseudomonas fragi, 7.0-7.2 (175), and Micrococcus, 8.0-8.5 ( 278). The pH optima of lipases of Penicillium roqueforti vary with the strain (170) the lipases of the mycelium and the lipases... [Pg.216]

Lipase is active at very low temperatures even in systems frozen solid at —15° (286, 287). Lipases of Pseudomonas fragi. Staphylococcus, and Penicillium caused measurable hydrolysis of emulsions of com oil, coconut oil, and lard in 2-4 days at —7°, in 7 days at —18°, and in 21 days at — 29° (288). [Pg.217]


See other pages where Pseudomonas fragi is mentioned: [Pg.824]    [Pg.201]    [Pg.100]    [Pg.683]    [Pg.731]    [Pg.732]    [Pg.824]    [Pg.1972]    [Pg.72]    [Pg.73]    [Pg.237]    [Pg.548]    [Pg.12]    [Pg.1972]    [Pg.537]    [Pg.34]    [Pg.39]    [Pg.1972]    [Pg.1462]    [Pg.1510]    [Pg.1008]    [Pg.100]    [Pg.180]    [Pg.229]    [Pg.208]    [Pg.681]    [Pg.218]    [Pg.156]   
See also in sourсe #XX -- [ Pg.9 ]




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