Preventive Nutrition and Food Science

The Korean Society of Food Science and Nutrition (한국식품영양과학회)
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Studies on Heated Protein Quality Using Homoarginine Method

  • Lee, Kyung--Hee (Dept. of Food and nutrition. Chang-won National University, Chang-Won 641-773) ;
  • Hel (Institut f r Humanern hrung und Lebensittelkunde, D sterbrooker Weg 17, 24105 Kiel, Germany)
  • Published : 1996.06.01
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Abstract

To determine the quality of heated protein, in vitro method, invluding lysine, lysionalanine, and fructose-lysine as well as homoarginine by guanidination of lysine, was assessed using heated casein with of without glucose. In vivo methods such as PER, digestibility and BV were also tried on homoarginine, lysinoalanine, fructoselysine, and lysine. The nonreactive lysine for huanidination was hardly digestive, while the non heat damaged lysine side chanis in the protein were accessible for guanidination as well as for the digestion. A linear correlation(${\gamma}$=0.80) was obstained between PER and digestibility of the analysed lysine. Digestibility of homoarginine was higher that of true protein. However, in the guanidinated heated casein with glucose, digestibility of homoarginine was significantly reduced. It is suggested that the homoarginine method may mislead to over- or underestimation of the damaged protein quality.

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References

  1. Proceeding of the Nutrition Society v.44 Chemical labelling of dietary protein by transformation of lysine to homoarginine ; a new technique to follow intestinal digestion and absorption Hagemeister,H.;Erbersdobler,H.
  2. Paper presented at 6th International Congress of Nutrition Guanidination, an alternative approach to the determination of available lysine in food Mauron,J.;Bujard,E.
  3. J. Food Science v.46 Measurement of available lysine using the guanidination reaction Maga,J.A.
  4. J. Nutr. v.121 Homoarginine labeling is suitable for determination of protein absorption in Miniature Pigs Schmitz,M.;Hagemeister,H.;Erbersdobler,H.
  5. Milk proteins Reliability and limitation of the homoarginine method for evaluation of protein digestibility in the pig Hagemeister,H.;Schmitz,M.;Erbersdobler,H.;Barth,C.A.(ed.);Schlimme,E.(ed.)
  6. Protein in human nutrition The use of ileal content analysis to assess the digestibility of amino acids Carpenter,K.J.;Porrer,E.(ed.);Rolls,P.(ed.)
  7. Arch. Bioch. Biophy. v.123 Lysine, homocitrulline. and homoarginine metabolism by the isolated perfused rat liver Ryan,W.L.;Barak,A.J.;Johnson,R.J.
  8. J. Nutr. v.105 Urea, citrate and orotate excretions in growing rats fed amino acid deficient diets Prior,R.L.;Milner,J.A.;Visek,W.J.
  9. J. Biol. Chem. v.183 New synthesis of a α-amino-ε-guanidino-n-carproic acid(Homoarginine) and its possible conversion in vivo into lysine Stevens,C.M.;Bush,J.A.
  10. Nutrition Report International v.36 Food choices and meal patterns of rats selecting from amino acid diets containing homoarginine Tews,J.K.;Repa,J.J.;Lichy,R.;Harper,A.E.
  11. Ph.D. Dissertation, Institut fur Physiologie und Biochemie der Ernahrung der Bundesanstalt fur milchforschung in Kiel Moglichkeit und grenzen der homoargininrnmarkierungsmetode zur verdaulichkeitsmessung von proten beim schwein Schmitz,M.
  12. Tierschutzgesetz 7833-3
  13. Z. Ernahrungswiss v.30 Determination of lysine damage and calculation of lysine bioavailability in several processed foods Erbersdobler,H.F.;Hupe,A.
  14. Am. J. Phys. v.222 Amino acid imbalance, protein intake, and changes in the rat brain and plasma amino acid Peng,Y.;Tews,J.K.;Harper,A.E.
  15. J. Nutr. v.118 Dietary amino acid analogues and transport of lysine or valine across the blood-brain barrier in rats Tews,J.K.;Greenwood,J.;Pratt,O.E.;Harper,A.E.
  16. J. Sci. Food Agric. v.47 In-vitro determination of nitrogen digestibility and lysine availability in meat and bone meals and comparison with in-vivo ileal digestibility estimates Moughan,P.J.;Schrama,J.;Skilton,G.A.;Smith,W.C.
  17. Food Chemistry v.3 Gas chromatographics determination of available lysine Nair,B.M.;Laser,A.;Burvall,A.;Asp,N.G.
  18. Nutrient availability, Chemical and biological aspects Factors influencing uptake and utilization of macronutrients Erbersdobler,H.F.;Southgate,D.A.T.(ed.);Johnson,I.T.(ed.);Fenwick,G.R.(ed.)
  19. British J. Nutr. v.26 Metabolism of heat damaged proteins in the rat Ford,J.E.;Shorrock,C.
  20. Z. Tierphyiol. Tierernahrung und Futtermittelkunde v.28 Uber Untersuchungen zur intestinalen Resorption von Epsilon-Fructoselysine Erbersdobler,H.F.
  21. Prog. Fd. Nutr. Sci. v.5 Transport and metabolism studies with fructoseamino acids Erbersdobler,H.F.;Brandt,A.;Scharrer,F.;Von Wangenheim, B.
  22. J. Agric. Food Chem. v.39 In vitro determination of the extent of hydrolysis of homoarginine by arginase in the small intestine of the growing rat Schuttert,G.;Moughan,P.J.;Jackson,F.
  23. Fette, Seifen, Anstrichmittel v.57 Die nicht enzymatische Braunung von Lebensmitteln Ⅱ Gornhart,L.
  24. Nutrition Abstracts and Reviews v.53 Lysinoalanine in food proteins Finot,P.A.
  25. Fd. Cosmet. Toxicol. v.17 Lysinoalanine formation in alkali-treated proteins and model peptides Karayiannis,N.I.;MacGregor,J.T.;Bjeldanes,L.F.
  26. Protein crosslinking. nutritional and medical consequences v.86B Availability of the true Schiff's bases between lysine and lactose in milk Finot,P.A.;Bujard,E.;Mottu,F.;Mauron,J.;Friedman,M.(eds.)