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  • 1
    Electronic Resource
    Electronic Resource
    Initial reactions in the oxidation of naphthalene by Pseudomonas putida (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 575-584 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00674a018
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Heat-Stable Proteases on the Kinetic Parameters of Milk Clotting by Chymosin (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The milk clotting per unit casein hydrolytic activities of proteases from 14 psychrotrophic pseudomonad isolates of raw milk ranged from 0.77 to 9.97 at 30°C. The milk clotting activities of chymodn and T16 protease were not completely additive, especially at high chymosin concentration when clotting time was relatively fast. The T16 protease was not effective in catalyzing the enzymic step of milk clbtting at O°C in the time expected on the basis of its milk clotting at 30°C. Milk incubated with the T25 motease for 8 days at 4°C and then clotted with chymosin at 30°C exhibited weak curd consistency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13754.x
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  • 3
    Electronic Resource
    Electronic Resource
    Initial steps of phloroglucinol metabolism in Penicillium simplicissimum (1990)
    Springer
    Archives of microbiology 153 (1990), S. 438-443 
    Details
    ISSN: 1432-072X
    Keywords: Penicillium simplicissimum ; Species description ; Phenolic compounds ; Phloroglucinol ; Aerobic degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The pathway for the aerobic catabolism of 1,3,5-trihydroxybenzene (phloroglucinol) by a new strain of Penicillium was investigated using both in vivo and in vitro cell-free systems. The fungal strain was isolated by enrichment on phloroglucinol and identified as P. simplicissimum (Oud) Thom. It grew optimally at pH 5.5 and 27°C with 119 mM (1.5%w/v) of phloroglucinol in a basal mineral salts medium. Vapours of the crystalline substrate placed in a Petri-plate lid supported the growth of the fungal colonies on the agar surface. Mycelia grown on phloroglucinol accumulated 1,2,4-trihydroxybenzene and resorcinol in the medium. Washed, resting mycelia grown on phloroglucinol, when resuspended in a buffer utilized oxygen in the presence of catechol, resorcinol, pyrogallol and phloroglucinol. A NADPH-dependent reductase in the cell-free extract reduced phloroglucinol to dihydrophloroglucinol. This electron donor could not be replaced by NADH. Resorcinol hydroxylase, phloroglucinol reductase, catechol-1,2-oxygenase, and catechol-2,3-oxygenase were detected in cell-free extracts of mycelia grown on phloroglucinol. The possible steps in the degradation of phloroglucinol are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248424
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  • 4
    Electronic Resource
    Electronic Resource
    Detoxification mechanisms for 1,2,4-benzenetriol employed by a Rhodococcus sp. BPG-8 (1993)
    Springer
    Archives of microbiology 159 (1993), S. 136-140 
    Details
    ISSN: 1432-072X
    Keywords: 1,2,4-Benzenetriol ; 2-hydroxy-1,4-benzoquinone ; Rhodococcus BPG-8 ; NAD(P)H-Dependent reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Rhodococcus sp. BPG-8 produces 1,2,4-benzenetriol during the transformation of resorcinol by phloroglucinol induced cell-free extract. The oxidation of 1,2,4-benzenetriol to 2-hydroxy-1,4-benzoquinone produces superoxide radicals that may have potential deleterious effects on cellular integrity. It has been shown that both superoxide dismutase (SOD) and catalase retard the autoxidation of 1,2,4-benzenetriol to 2-hydroxy-1,4-benzoquinone. Termination of the free radical chain reaction between superoxide radical and 1,2,4-benzenetriol seems to prevent this autoxidation. A NAD(P)H-dependent reductase appears to convert the 2-hydroxy-1,4-benzoquinone back to 1,2,4-benzenetriol. Both of these mechanisms appear to stabilize 1,2,4-benzenetriol so that it may be cleaved by meta cleavage enzymes. The enzymes responsible for the stabilization of 1,2,4-benzenetriol appear not to be inducible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00250273
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    Paper (German National Licenses)
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