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  • 1
    Electronic Resource
    Electronic Resource
    The accelerating effect of aLactococcus lactis subsp.lactis lactose-utilization/proteinase-deficient strain on proteolysis and flavour development (1996)
    Springer
    European food research and technology 203 (1996), S. 77-81 
    Details
    ISSN: 1438-2385
    Keywords: Lactococci ; Proteolysis ; Flavour development ; Cheese-curd slurries
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract This study describes the accelerating effect exerted on proteolysis and flavour development in cheese-curd slurries by combined application ofLactococcus lactis subsp.lactis IFPL359 and high concentrations of its Lac− Prt− derivative, (i.e. that which has reduced capacity to metabolize lactose and reduced proteolytic activity, strain T1). Cells of strain T1 partially lysed by either sonication or incubation with lysozyme, were also used to ascertain how proteolysis was affected by release of intracellular enzymes in the initial stage of incubation of the strains in cheese-curd slurries. The presence of strain T1 produced higher levels of non-protein nitrogen (NPN) and amine nitrogen (AN) during the first weeks of incubation when partially lysed cells had been added. Addition of whole cells of strain T1 produced higher values of NPN and AN at the end of incubation of slurries, accelerating proteolysis by about 2 weeks with respect to the control, which only contained the parental strain IFPL359. At the end of the experimental period higher amino acid levels were detected by HPLC in the slurry containing whole T1 cells. Volatile fractions of the different cheese-curd slurries were also analysed. The higher level of proteolysis produced by addition of high levels of strain T1 appeared to be related to release of intracellular enzymes by this strain owing to its greater capacity for autolysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01267774
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  • 2
    Electronic Resource
    Electronic Resource
    A reinvestigation of the Gn-RH (gonadotrophin-releasing hormone) systems in the goldfish brain using antibodies to salmon Gn-RH (1986)
    Springer
    Cell & tissue research 244 (1986), S. 327-337 
    Details
    ISSN: 1432-0878
    Keywords: Gonadotrophin-releasing hormone ; Teleosts ; Immunohistochemistry ; Neuroendocrine control ; Reproduction ; Goldfish (Carassius auratus)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The organization of Gn-RH systems in the brain of teleosts has been investigated previously by immunohistochemistry using antibodies against the mammalian decapeptide which differs from the teleostean factor. Here, we report the distribution of immunoreactive Gn-RH in the brain of goldfish using antibodies against synthetic teleost peptide. Immunoreactive structures are found along a column extending from the rostral olfactory bulbs to the pituitary stalk. Cell bodies are observed within the olfactory nerves and bulbs, along the ventromedial telencephalon, the ventrolateral preoptic area and the latero-basal hypothalamus. Large perikarya are detected in the dorsal midbrain tegmentum, immediately caudal to the posterior commissure. A prominent pathway was traced from the cells located in the olfactory nerves through the medial olfactory tract and along all the perikarya described above to the pituitary stalk. In the pituitary, projections are restricted to the proximal pars distalis. A second immunoreactive pathway ascends more dorsally in the telencephalon and arches to the periventricular regions of the diencephalon. Part of this pathway forms a periventricular network in the dorsal and posterior hypothalamus, whereas other projections continue caudally to the medulla oblongata and the spinal cord. Lesions of the ventral preoptic area demonstrate that most of the fibers detected in the pituitary originate from the preoptic region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00219208
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  • 3
    Electronic Resource
    Electronic Resource
    Gas-phase thermolysis of N-methyl-N-phenyl-tert-butylsulfenamide and morpholinyl-tert-butylsulfenamide (1998)
    Chichester : Wiley-Blackwell
    Journal of Physical Organic Chemistry 11 (1998), S. 407-410 
    Details
    ISSN: 0894-3230
    Keywords: gas-phase thermolysis ; N-methyl-N-phenyl-tert-butylsulfenamide ; morpholinyl-tert-butylsulfenamide ; Chemistry ; Theoretical, Physical and Computational Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: N-Methyl-N-phenyl-tert-butylsulfenamide (MPSA) and morpholinyl-tert-butylsulfenamide (MOSA) were thermolyzed in a stirred-flow reactor at temperatures of 340-390 °C and pressures of 7-13 Torr, using toluene as carrier gas, at residence times of 0.3-1.3 s. Isobutene was formed in 99% yield through first-order reactions having the following Arrhenius parameters (A,s-1, Ea, kJ mol-1): MPSA, log A  =  12.41 ± 0.02, Ea  =  158.8 ± 0.2; MOSA, log A  =  12.91 ± 0.22, Ea  =  159 ± 3. It is proposed that the elimination of isobutene takes place by unimolecular reaction mechanisms involving polar, four-center cyclic transition states, forming S-unsubstituted thiohydroxylamines as co-products. Thermochemical parameters, estimated by semiempirical AM1 calculations, are reported for the latter and for the parent molecules. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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