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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 39 (1991), S. 1444-1447 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Selenium ; Hydrogenase ; Bradyrhizobium japonicum ; Nitrogen fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It has been established that the hydrogenase from autotrophically cultured Bradyrhizobium japonicum contains selenium as a bound constituent. About 80% of the enzyme selenium remains bound during precipitation with 5% trichloroacetic acid (TCA). However, 85% of the selenium bound to the enzyme is released by a combined treatment of urea, heat and TCA. Neither selenomethionine nor selenocysteine could be detected on analysis of anaerobically hydrolyzed enzyme. These results are consistent with the report showing that the structural genes for this enzyme do not contain a TGA codon (Sayavedra-Soto et al. 1988) which has been reported to code for selenocysteine incorporation into several proteins (Chambers et al. 1986; Zinoni et al. 1986; Stadtman 1987). We have demonstrated that 75Se from the labeled hydrolyzed enzyme forms the derivative' selenodicysteine. The form of selenium resulting in the synthesis of this derivative apparently is SeO inf3 sup= or a compound such as Se= which is easily oxidized to SeO inf3 sup= . In a separate approach it was established that 12–16% of the total 75Se in the native enzyme reacted with 2,3-diaminonaphthalene indicating that this fraction was present as SeO inf3 sup= . The remaining 75Se was bound to the enzyme protein. From this research, we concluded that Se in Bradyrhizobium japonicum hydrogenase is present in a labile bound form. In this respect, this enzyme is similar to xanthine dehydrogenase and nicotinic acid hydroxylase, both of which contain labile Se constituents that have not been defined.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: ?Anjou, Comice, and Bartlett pears were processed into clarified juices from hard green and soft ripened fruits. Processing trials with and without SO2 were conducted. Effects of variety, maturity and processing on browning, turbidity, proteins, and stability were investigated. Browning increased with heat treatment, and was reduced by processing with SO2. Total soluble protein content increased with fruit maturity and processing with SO2. Protein fractions from a clarifying enzyme preparation (mainly arabinase and amylase) with MW in the range of 64,000–92,000 and containing glycoproteins were not removed by fining/clarification. They contributed to protein instability in the clarified pear juices, but could be removed by heat treatment (pasteurization) prior to final filtration and bottling. Our results indicate some enzymes added for clarification during processing may contribute to post-clarification haze and sediment formation.
    Type of Medium: Electronic Resource
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