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  • 1960-1964  (26)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 26 (1961), 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: Application of the 2,4-dinitrophenylhydrazine method of Roe and co-workers to plant extracts, wherein ascorbic acid was present largely or completely in the form of DHA and DKA, resulted in abnormal data, in the sense that the value of AA + DHA + DKA was significantly lower than that of DHA + DKA. Such a discrepancy, though not to the same degree, was observed also when the analyses were carried out on solutions of DHA. The loss is believed to take place during H2S treatment, there being a correlation between the extent of loss and the duration of H2S treatment, in the majority of the experiments.
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 26 (1961), 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: Homogenates of plant material were examined for enzymatic delactonization of dehydroascorbic acid and oxidation of diketogulonic acid. Bitter gourd fruit, cauliflower, and the leaves of the tapioca plant contain an enzyme that brings about conversion of dehydroascorbic acid to diketogulonic acid. Tapioca leaves are able to effect, in addition, a significant enzyme-catalyzed degradation of diketogulonic acid. The 1eaves of the tapioca plant contain some material that stabilizes ascorbic acid against oxidation to dehydroascorbic acid during homogenization in a Waring blender.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 39 (1961), S. 335-342 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Lyophilized and stored in a deep-freeze, the mycelial material was found to retain cis-aconitic decarboxylase activity unimpaired at the end of 2 months. Mycelia could be stored also in the frozen condition but after squeezing hard to remove as much of adherent water as possible. Extracts with maximum cis-aconitic decarboxylase activity were obtained when the frozen or better the lyophilized mycelia of Aspergillus terreus were ground in a mortar with phosphate buffer using pyrex glass powder as abrasive. Cis-aconitic decarboxylase was purified 25-fold by fractionation with ammonium sulfate, starting from extracts of the mycelia in phosphate buffer. The purified enzyme was considerably more stable than the crude extracts to storage and dialysis. The optimum pH was 5.8 using 0.2 m phosphate buffer; Km value was 5×10-3 m at pH 5.8 and 37°C. EDTA and 8-hydroxyquinoline activated the enzyme; all metals tested inhibited the enzyme, Zn++ and Cu++ leading to complete inactivation. Fluoride, arsenite and azide also inhibited the enzyme activity.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 39 (1961), S. 343-350 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 46 (1963), S. 409-413 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Catalase of spores of Aspergillus niger is an insoluble enzyme. It appears to be localized on particles sedimenting at low relative centrifugal forces.
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  • 6
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 191 (1961), S. 516-517 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The transaminase activity was determined by the colorimetric method of Tonhazy et al2 on homogenates of pooled samples of phylloclades collected at 4-hourly intervals over a 24-hr. period in February and in March of this year. A unit of enzyme was defined as the amount which gave rise to 1 μgm. ...
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  • 7
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 193 (1962), S. 166-167 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A representative number of leaflets were gathered every 4 hr. during a 24-hr, period from tapioca plants grown under natural conditions of light and darkness in garden soil. A 20 per cent homogenate in water was prepared by the use of a Waring blender and aliquots used for enzyme and other assays. ...
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  • 8
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 188 (1960), S. 664-665 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Nopalea dejecta used in the experiments was grown in the open, in garden soil. Aldolase activity was assayed by the method of Sibley and Lehninger4. The activity of the enzyme was expressed in mm.3 of fructose-1 : 6-diphosphate split in 30 min. at pH. 8.6. Phosphatase activity, using pre-adjusted ...
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  • 9
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 188 (1960), S. 144-144 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A search by us has shown that cauliflower (Brassica oleracea botrytis) and bitter gourd (Momordica charantia) possess an enzymatic mechanism for the conversion of dehydroascorbic acid to diketogulonic acid. The technique of investigation consisted in incubating homogenates with dehydroascorbic acid ...
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 49 (1964), S. 183-192 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. A study has been made of the catalase activity of the spores of Aspergillus niger, NRRL 599. The enzyme occurs in 2 forms in the spores: (a) readily accessible, as evidenced by the activity of untreated whole spores and (b) difficultly accessible, as represented by that component which becomes fully reactive when the spores are disrupted or reactive to varying degrees on treatment with dioxane or one of the surface active agents, deoxycholate, digitonin and triton X-100. The latter form constitutes over twice the former. Barring dioxane treatment, conventional techniques failed to solubilize the enzyme. 2. The two forms of catalase differ in some properties, the most important of which is the behaviour on heating for 5 min at 70°C. The accessible form undergoes inactivation to a considerable extent, whereas the inaccessible form is not significantly affected. The heat sensitive part of catalase tends to be associated with particles sedimenting from aqueous homogenates at the lowest relative centrifugal forces. The accessible form is also preferentially sensitive to storage at room temperature or in a Deep-freeze. A part of the accessible form is soluble in dioxane; the rest is insoluble. However, no distinction between the two forms was demonstrable on the basis of pH-activity relationship or inhibition by cyanide and fluoride. 3. These properties could be largely accounted for by assuming that the greater part of catalase of spores is firmly bound to structural elements in the spores such as the spore coat and that the rest is east is easily accessible by occurring at the openings on this structure.
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