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Gas chromatographic evaluation of amino acid epimerisation in the course of gelatin manufacturing and processing

  • M. Lüpke
  • H. Brückner
ORIGINAL PAPER

Abstract

 Using capillary gas chromatography on chiral stationary phases total hydrolysates of gelatins were investigated for their amounts of D-amino acids (D-AAs). Gelatins of different quality and origin were analysed including gelatin-containing final products like candies and meat products. In gelatins manufactured by stepwise extraction (first to fifth extract) with water of increasing temperature (ca. 55–95°C) amounts of 2.7–4.8% of D-aspartic acid (D-Asp) were determined in extracts obtained at ≤ 85°C. The amounts D-Asp were as high as 28.1% in fifth extracts obtained at 95°C (data corrected for 4.3% of D-Asp determined in native collagen as a result of acid-induced epimerisation of L-Asp during total hydrolysis). Epimerisation of aspartyl or asparaginyl residues of proteins in general on heating in water is assumed to proceed via formation of aspartyl succinimide, tautomerisation and release of D-Asp on total hydrolysis. The other AA residues of gelatin showed only a slight increase of epimerisation with increasing thermal treatment. Furthermore, amounts of 3–4% of cis-4-D-hydroxyproline, formed from native trans-4-L-hydroxyproline in collagen on hydrolysis, were detected in total hydrolysates of all gelatins.

Key words Collagen D-Amino acids Hydroxyproline stereoisomers Racemisation Food proteins 

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • M. Lüpke
    • 1
  • H. Brückner
    • 2
  1. 1.Institute of Food Technology, University of Hohenheim, D-70593 Stuttgart, GermanyDE
  2. 2.Institute of Nutritional Science, Department of Food Sciences, University of Giessen, D-35390 Giessen, GermanyDE

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