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  • 1
    Electronic Resource
    Electronic Resource
    Efficient determination of individual maillard compounds in heat-treated milk products by amino acid analysis
    Amsterdam : Elsevier
    International Dairy Journal 1 (1991), S. 125-135 
    Details
    ISSN: 0958-6946
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0958-6946(91)90004-R
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Book reviews (1994)
    Springer
    European food research and technology 199 (1994), S. 322-324 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01193320
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  • 3
    Electronic Resource
    Electronic Resource
    Relationship between the crosslinking of caseins by transglutaminase and the gel strength of yoghurt (2000)
    Springer
    European food research and technology 210 (2000), S. 305-309 
    Details
    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
    URL: http://dx.doi.org/10.1007/s002170050554
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  • 4
    Electronic Resource
    Electronic Resource
    Book reviews (1995)
    Springer
    European food research and technology 201 (1995), S. 99-104 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01193210
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Book reviews (1995)
    Springer
    European food research and technology 201 (1995), S. 411-415 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01192743
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Detection and quantification of pentosidine in foods (1997)
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 204 (1997), S. 95-98 
    Details
    ISSN: 1431-4630
    Keywords: Key words Pentosidine ; Maillard reaction ; Amino acid analysis ; Crosslinking ; Proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Pentosidine, a crosslink amino acid in which one arginine and one lysine residue are linked together by a pentose, has been detected in foods for the first time using ion-exchange chromatography with direct fluorescence detection and subsequent ninhydrin derivatization. The method allows the simultaneous quantification of pentosidine along with all other amino acids of acid hydrolyzates at levels lower than 50 μg kg protein. Levels of pentosidine in all food samples investigated were very low (milk products between not detectable and 2–5 mg/kg protein; roasted coffee and some bakery products up to 35 mg/kg protein), indicating that pentosidine does not play a major part in the polymerization of food proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002170050043
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  • 7
    Electronic Resource
    Electronic Resource
    Formation of thiazolines within the peptide chain during heating of proteins (1997)
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 204 (1997), S. 247-251 
    Details
    ISSN: 1431-4630
    Keywords: Key words Thiazolines ; 2-Methyl-4-carboxy-thiazoline ; Backbone modification ; Proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract   L-2-Methyl-4-carboxy-thiazoline was isolated by ion-exchange chromatography and RP-HPLC from heated solutions of N-acetyl-L-cysteine. The structure was established by NMR-spectroscopy. The formation of thiazolines during the heating of cysteine-containing peptides (glycyl-glycyl-cysteine, glycyl-cysteinyl-glycine, glutathione) was observed by UV and NMR-spectroscopy and measured by cation-exchange chromatography. The rate of formation was dependent on the pH, the water activity and the temperature. In comparison with untreated samples, a characteristic increase of absorption at 260 nm in heated proteins (β-lactoglobulin, ovalbumin) was noticed. Using NMR-spectroscopy [two-dimensional: hetero nuclear multiple quantum coherence (HMQC) and total correlated spectroscopy (TOCSY)] the formation of thiazolines within heated proteins (β-lactoglobulin, egg white albumin and bovine serum albumin) could be demonstrated unequivocally. The signals of the methine-proton of thiazolines as well as the coupling constants of the thiazoline protons are very characteristic and not overlaid by signals of protein-bound amino acids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002170050072
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  • 8
    Electronic Resource
    Electronic Resource
    On the reaction of glyoxal with proteins (1997)
    Springer
    Zeitschrift für Lebensmittel-Untersuchung und -Forschung 205 (1997), S. 121-124 
    Details
    ISSN: 1431-4630
    Keywords: Key words Arginine ; Glyoxal ; Maillard reaction ; Protein modification ; 1-(4-Amino-4-carboxybutyl)-2-imino-5-oxo-imidazolidine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The reaction of arginine and arginine derivatives with glyoxal under mild conditions revealed the formation of a previously unknown amino acid, designated as “Glarg”. 1H-, 15N- and 13C-NMR analysis of the new compound elucidated its structure to be 1-(4-amino-4-carboxybutyl)-2-imino-5-oxo-imidazolidine. Experiments with solutions containing N α -acetylarginine and glyoxal showed that “Glarg” is formed quickly under physiological conditions, but is labile at higher temperatures as well as at low pH values. After incubation of β-casein with glyoxal, the formation of protein-bound “Glarg” in enzymatic hydrolysates via amino acid analysis could be demonstrated. Due to the fast reaction of glyoxal with arginine residues, under physiological conditions, proteins may act as scavengers for glyoxal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002170050137
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