Süt ve Süt Ürünlerinde Bir Kalite Parametresi: Lisinoalanin

Lisinoalanin LAL , bazik bir aminoasit olup gıdalarda ısıl tahribatın bir göstergesi olarak kullanılır. LAL oluşumunda gıdanın bileşimi, üretim ve depolama koşulları gibi birçok faktör etkili olsa da, alkali ile muamele, yüksek sıcaklıklarda işlem ile açık bir şekilde korunaksız depolama gibi faktörler protein içeren gıdalarda LAL oluşumunu teşvik eden en önemli etmenler arasındadır. LAL tahıl ürünleri, tavuk eti, yumurta ürünleri, jelatin, bebek mamaları, et ürünleri, kazeinat, soya proteini izolatı, UHT süt, süttozu ve peynir gibi yaygın olarak tüketilen gıdalarda bulunabilmektedir. Esansiyel aminoasitlerin azalması, protein kalitesinin, mineral madde biyoyararlılığının düşmesi ve meydana gelebilecek toksikolojik etkiler LAL oluşumundan kaynaklanan olumsuz sonuçlardan bazılarıdır. Bu nedenle gıda işleme sırasında LAL oluşumunu minimize etmek için stratejiler geliştirilmelidir. LAL, gıda endüstrisinde Maillard Reaksiyon ürünlerine kıyasla daha iyi bir kalite göstergesi olarak kabul edilmektedir. Ayrıca gıda maddesine kazeinat ilave edilmesi gibi durumlarda kalite indeksi olarak da kullanılabilmektedir. Yapılan çalışmalara bakıldığında ise süt ve süt ürünlerinde LAL’in tespiti ile ilgili bilgilerin yetersiz olduğu görülmektedir

Lysinoalanine: A Quality Parameter for Milk and Dairy Products

Lysinoalanine LAL is an alkali amino acid and has been used as a marker of thermal damage in foods. Many factors can be effective in its formation such as composition of food and manufacture and storage conditions. However, alkali treatment, processing at high temperature and uncovered and unprotected storage are among the most effective factors, and these can lead to the formation of LAL in foods containing protein. LAL can be found in numerous foods such as cereals, chicken, egg, gelatin, infant formulas, meat products, caseinate, soy protein isolate, UHT milk, milk powder and cheese. Negative effects of the formation of LAL on foods include a reduction in essential amino acids contents of foods, a decrease in protein quality and bioavailability of minerals and the occurrence of toxicological effects. Therefore, strategies should be developed to minimize LAL formation during food processing. LAL has been widely accepted as a better quality parameter in food industry than Maillard Reaction products. Furthermore, it can be also used as a quality index when caseinate is added to food. Further studies should focus on the determination of LAL in milk and dairy products

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  • Faist V., Drusch S., Kiesner C., Elmadfa I., Erbersdobler H.F., 2000. Determination of lysinoalanine in foods containing milk protein by high-performance derivatisation with dansylchloride. International Dairy Journal 10: 339-346. after
  • Hayashi, R., 1982. Lysinoalanine as a metal chelator. The Journal of Biological Chemistry 257: 13896-13898.
  • Woodard, J.C., Short, D.D., 1973. Toxicity of alkali-treated soy proteins in rats. Journal of Nutrition 103: 569-574.
  • de Groot A.P., Slump P., Feron V.J., van Beek L., 1976. Effects of alkali-treated proteins: Feeding studies with free and protein-bound lysinoalanine in rats and other animals. Journal of Nutrition 106: 1527-1538.
  • Pfaff G., 1984. Lysinoalanine contents of formula diets. Lancet I 448.
  • Faist, V., Wenzel, E., Tasto, S., Müller, C., Erbersdobler, H. F., 1998. Tissue specific induction of phase I and II xenobiotic enzymes and oxygen free radical metabolism in rats fed alkali- treated protein containing high levels of lysinoalanine. FASEB J., 13: 1268.
  • Lee, K.-H., Erbersdobler, H. F., 1994. Balance experiments on human volunteers with ε- fructoselysine and lysinoalanine. In: Maillard reactions in chemistry, food and health. Proceedings of the fifth international symposium on Maillard Browning (Ed. T. P. Labuza, G. A. Reineccius, V. M. Monnier, J. O‘Brien & J. W. Baynes). The Royal Society of Chemistry, Cambridge, 358-363.
  • Antila P., Pullinen E., Antila V., 1987. The formation and determination of lysinoalanine in foods containing milk protein. Finnish Journal of Dairy Science 45: 1-18.
  • Badoud R., Pratz G., 1984. Simple and rapid quantitative determination of lysinoalanine and protein hydrolysate amino acids by high- performance derivatization Chromatographia 19: 155-164. dansyl with chloride.
  • Moret S., Cherubin S., Rodriguez-Estrada M.T., Lercker G., 1994. Determination of lysinoalanine by high performance liquid chromatography. Journal of High Resolution Chromatography 17: 827-830.
  • Wood-Rethwill J.C., Warthesen J.J., 1980. Lysinoalanine determination in proteins using high-pressure liquid chromatography. Journal of Food Science 45: 1637-1640.
  • Pellegrino L., Resmini P., Denoni I., Masotti F., 1996. Sensitive determination of lysinoalanine for distinguishing natural from imitation mozzarella cheese. Journal of Dairy Science 79: 725-734.
  • Fenaille F., Parisod V., Visani P., Populaire S., Tabet J.C., Guy P.A., 2006. Modifications of milk constituents during processing: A preliminary benchmarking study. International Dairy Journal 16: 728-739.
  • Cattaneo, S., Masotti, F., Pellegrino, L., 2008. Effects of overprocessing on heat damage of UHT milk. European Food Research and Technology 226: 1099-1106.
  • Hasegawa K., Mukai K., Gotoh M., Honjo S., Matoba T., 1987. Determination of the lysinoalanine content in commercial foods by gas chromatography-selected Agricultural and Biological Chemistry 51: 2889- 2894. ion monitoring.
  • Henle T., Walter A.W., Klostermeyer H., 1993. Detection and identification of the cross-linking amino acids Nт- and Nтт-(2’-amino-2’-carboxy- ethyl)-L-histidine («histidinoalanine», HAL) in heated milk products. Zetschrift für Lebensmittel Untersuchungen und Forschung 197: 114-117.
  • Sieber, R., Bütikofer, U., Kaldas, N., Rehberger, B., 2007. Vorkommen von Lysinoalanin in Milch und Milchprodukten. ALP science, Nr. 509.
  • Holstein, A.B., 1979. Modelluntersuchungen über die Bildung von Lysinoalanin bei Hitzebehandlung von München 79S. Universitaet
  • Fritsch R.J., 1984. Analytik, entstehen und von vorkommen milcheiweisshaltigen Milchwirtschaft 35: 1932-1935. in
  • lebensmitteln. Deutsche
  • Friedman, M., 1999. Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. Journal of Agricultural and Food Chemistry 47(4): 1295-1319.
  • Meyer M., Klostermeyer H., Kleyn D.H., 1981. Reduced enzymaticaly dephosphorylated casein. Zeitschrift für Lebensmittel Untersuchungen und Forschung 172: 446-448. of lysinoalanine in
  • Steining, J., Montag, A., 1982. Studies on changes in lysine of food proteins. II. Formation of lysinoalanine. Untersuchungen und Forschung 175: 8-12.