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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 13 (1974), S. 5395-5400 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of food science & technology 16 (1981), S. 0 
    ISSN: 1365-2621
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The solubility of wheat gluten may be increased greatly by treatment with 0.25 M sodium hydroxide. At temperatures of 40°C and above, the solubility of the protein exceeds 100 mg/ml in a reaction time of 6 hr or less. The products from the reaction of 60°C and 80°C were darker than the original gluten and had an unpleasant odour of H2S on dissolution in water. They also contained traces of lysinoalanine. The 40°C reaction product was about the same colour as gluten, and its solutions in water did not smell of H2S. Reaction of gluten at 20°C also caused a large increase in solubility, but after 24 hr the solubility was only 77 mg/ml. This product was also of the same colour as gluten, and did not smell of H2S in solution. Neither the 20°C nor the 40°C products contained detectable traces of lysinoalanine. For reasons of flavour, colour, lysinoalanine content and economy of time, the optimum reaction conditions are 6 hr at 40°C.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of food science & technology 19 (1984), S. 0 
    ISSN: 1365-2621
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: When vital wheat gluten is treated with 0.25 M sodium hydroxide, its solubility is greatly improved, permitting a protein solution in excess of 100 mg/ml in water. This product has proved useful for industrial and food uses, but for use in bland foods it suffers from the disadvantage of possessing a soapy taste. In an attempt to overcome this problem, flour was defatted by solvent extraction and gluten was handwashed from it. When this defatted gluten was treated with alkali under similar conditions, it lacked the soapy taste but it was rendered soluble to the extent of only 20–30 mg/ml. Alkali treatment of defatted gluten or normal gluten resulted in the deamidation of approximately the same amount of the total glutamine + asparagine residues in either case. The lack of solubility of the alkali-treated defatted gluten is attributed to the absence of sodium salts of fatty acids. It is proposed that the effectiveness of sodium hydroxide in solubilizing normal gluten is derived from the hydrolysis of the lipids present in gluten to their respective fatty acid salts. If the same high degree of solubility is to be retained, methods other than the treatment of defatted gluten must be used to overcome the flavour problem where necessary.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Molecular biology reports 2 (1975), S. 65-72 
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yeast tRNAPhe has been labelled with 125I under conditions which conserve the tertiary structure. Significant labelling was only found to occur on specific cytidines in single stranded regions, while other cytidines in single stranded regions and all those in the double stranded region underwent iodination to a very small extent. The pattern obtained from iodine labelling satisfies the conformation of a model recently proposed for this tRNA.
    Type of Medium: Electronic Resource
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