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  • Insulin  (1)
  • Key words Yoghurt  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European food research and technology 210 (2000), S. 305-309 
    ISSN: 1438-2385
    Keywords: Key words Yoghurt ; Transglutaminase ; Casein oligomerization ; Gel-permeation chromatography ; Isopeptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  After pre-incubation of skim milk with microbial transglutaminase (10.5 U/100 ml skim milk or 3 U/g milk protein) at 40  °C for 150 min and subsequent heat inactivation, yoghurt was prepared. The breaking strength of this yoghurt increased in the given system from 550 cN to 920 cN with increasing pre-incubation time, reaching a plateau after 60 min. This increase in breaking strength correlates with a rather small amount of casein oligomerization, ranging from 10.9% to 25.8% using gel-permeation chromatography under reducing and denaturing conditions (sum of predominantly formed dimers and trimers in the total casein fraction). After enzymatic hydrolysis, N ε-(γ-glutamyl)-l-lysine was quantified by amino acid analysis. The isopeptide was formed exclusively intermolecularly, indicating that even a very small amount of casein crosslinking is capable of inducing significant changes in the functional properties of milk proteins.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 5 (1966), S. 807-822 
    ISSN: 0570-0833
    Keywords: Insulin ; Hormones ; Proteins ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The protein hormone insulin occurs widely in the animal kingdom. Although its biological function is always the same, its amino-acid composition varies widely. Insulin consists of two polypeptide chains, which are linked by three cystine residues to form a bicyclic system with a 20-membered and an 85-membered ring. The protein crystallizes in various forms with foreign ions. In solution, insulin normally forms aggregates of 2n molecules. The hormone can be regenerated from the separated polypeptide chains, and its total synthesis has been achieved in a similar manner from synthesized peptide chains. In the biosynthesis of insulin, the two chains are evidently built up separately and subsequently linked together. Insulin promotes the synthesis of glycogen, fat, and protein in the organism; insulin deficiency leads to an increase in the blood-sugar level. At the molecular level, the mechanism of action of the hormone is still unknown. Current hypotheses are discussed. No specific active center has so far been detected in the insulin molecule, which contains several antigenic regions.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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