Studies on the thermal sensitivity of γ-glutamyl transpeptidase measured with a modified test procedure and compared with that of alkaline phosphatase and lactoperoxidase in milk

Lait

Volumn 82, Issue 5, 2002, Pages 555-566

  Blel, Mustapha ^a   Guingamp, Marie France ^a   Gaillard, Jean Luc ^a   Humbert, Gérard ^a  

^a UNIVERSITÉ DE LORRAINE   (France)

Author keywords

Alkaline phosphatase; Bovine milk; Cheese; Heat treatment; Lactoperoxidase; glutamyl transpeptidase

Indexed keywords

DAIRY PRODUCTS; HEAT TREATMENT; QUALITY CONTROL; SPECTROPHOTOMETRY; THERMAL EFFECTS;

PASTEURIZATION; THERMAL SENSITIVITY;

ENZYMES;

BOVINAE;

EID: 0036746784     PISSN: 00237302     EISSN: None     Source Type: Journal    
DOI: 10.1051/lait:2002032     Document Type: Article

References (31)

1. Allison R.D., γ-Glutamyl transpeptidase: Kinetics and Mechanism, Methods Enzymol. 113 (1985) 419-437.
2. Andrews A.T., Anderson M., Goodenough P.W., A study of heat stabilities of a number of indigenous milk enzymes, J. Dairy Res. 54 (1987) 237-246.
3. Baumrucker C.R., γ-Glutamyl transpeptidase of bovine milk membranes: distribution and characterization, J. Dairy Sci. 62 (1979) 253-258.
4. Baumrucker C.R., Purification and identification of γ-glutamyl transpeptidase of milk membranes, J. Dairy Sci. 63 (1980) 49-54.
5. Dos Anjos F., Machdo A., Ferro C., Bogin E., γ-Glutamyl transpeptidase as a marker for pasteurization of raw milk, J. Food Protect. 61 (1998) 1057-1059.
6. Farkye N.Y., Imafidon G.I., Thermal denaturation of indigenous milk enzymes, in: IDF Special Issue 9501, Heat induced changes in milk, Int. Dairy Fed., Brussels, Belgium, 1995.
7. Griffiths M.W., Use of milk enzymes as indices of heat treatment, J. Food Protect. 49 (1986) 696-705.
8. Guingamp M.F., Humbert G., Linden G., Determination of sulfhydryl groups in milk using Ellman's procedure and the Clarifying Reagent®, J. Dairy Sci. 76 (1993) 2152-2155.
9. Guingamp M.F., Blel M., Gaillard J.L., Humbert G., A rapid method for peroxidase activity in heated milk with the Clarifying Reagent®, Poster presentation in EURO FOOD CHEM IX, Federation of European Chemical Society, Authenticity and adulteration of food-the analytical approach, Interlaken, Switzerland, 1997.
10. Humbert G., Guingamp M.F., Kouomegne R., Linden G., Measurement of proteolysis in milk and cheese using trinitrobenzene sulfonic acid and a new dissolving reagent, J. Dairy Res. 57 (1990) 143-148.
11. Humbert G., Guingamp M.F., Choukri A., Linden G., Method for the measurement of Nacetyl-β-D-glucosaminidase activity in bovine milk, J. Dairy Res. 62 (1995) 369-372.
12. Humbert G., Guingamp M.F., Linden G., Method for the measurement of lipase activity in milk, J. Dairy Res. 64 (1997) 465-469.
13. Linden G., Pâquet D., Alkaline phosphatase activity in transparent milk and cream, J. Dairy Sci. 64 (1981) 568-571.
14. Linden G., Humbert G., Kouomegne R., Guingamp M.F., Reagent for rendering biological fluids transparent and its analytical applications, European patent application EP 0246 978 B1. 1987, 10p.
15. McKellar R.C., Influence of ice-cream mix components on the thermal stability of bovine milk γ-glutamyl transpeptidase and Listeria innocua, Int. Dairy J. 6 (1996) 1181-1189.
16. McKellar R.C., Emmons D.B., Farber J., γ-Glutamyl transpeptidase in milk and butter as an indicator of heat treatment, Int. Dairy J. 1 (1991) 241-251.
17. Monget D., Laviolette P., Mise au point de microtests phosphatase alcaline et peroxydase pour le contrôle de la pasteurisation du lait de vache, Lait 58 (1978) 595-605.
18. Murthy G.K., Cox S., Kaylor L., Reactivation of alkaline phosphatase in ultra high-temperature, short-time processed liquid milk products, J. Dairy Sci. 59 (1976) 1699-1710.
19. Olsewski E., Renter H., Das inaktivierungs-und reaktivierungsverhalten der lactoperoxidase in milch im temperaturbereich von 50 bis 135 °C. (The inactivation and reactivation behaviour of lactoperoxidase in milk at temperatures between 50 °C and 135 °C), Z. Lebensm. Unters. Forsch. 194 (1992) 235-239.
20. Orlowski M., Meister A., γ-Glutamyl-p-nitroanilide: A new convenient substrate for determination and study of L-and D-γ-glutamyl transpeptidase activities, Biochim. Biophys. Acta 73 (1963) 679-681.
21. Patel S.S., Wilbey R.A., Thermal inactivation of γ-glutamyl transpeptidase and Enterococcus faecium in milk-based systems, J. Dairy Res. 61 (1994) 263-270.
22. Pellegrino L., Resmini P., Luf W., Assessment (indices) of heat treatment of milk, in: IDF Special Issue 9501, Heat induced change in milk, Int. Dairy Fed., Brussels, Belgium, 1995.
23. Pellegrino L., Tirelli A., Masotti F., Resmini P., Significance of the main chemical indicators of heat load for characterizing raw, thermized, pasteurized and high temperature pasteurized milk, in: IDF Special Issue 9602, Heat treatment and alternative methods, Int. Dairy Fed., Brussels, Belgium, 1996.
24. Persijn J.P., Van Der Slik W., A new method for the determination of γ-glutamyltransferase in serum, J. Clin. Chem. Clin. Biochem. 14 (1976) 421-427.
25. Schlimme E., Kiesner C., Lorenzen P.C., Martin D., Influence of heat treatment of milk on the activities of the indigenous milk enzymes alkaline phosphatase and adenosine deaminase, Bull. Int. Dairy Fed. 332 (1998) 25-31.
26. Sharma R., Surendranath B., Sharma V., Indicators to assess the intensity of heat treatments in milk and milk products, Indian Dairyman 52 (2000) 45-52.
27. Shaw L.M., γ-Glutamyltransferase, in: Bergmeyer H.U. (Ed.), Methods of enzymatic analysis, (Vol. III), Verlag Chemie Weinheim, Germany, 1983, pp. 349-352.
28. Smith T.K., Meister A., Chemical modification of active site residues in γ-glutamyl transpeptidase, J. Biol. Chem. 270 (1995) 12476-12480.
29. Tate S.S, Meister A., γ-Glutamyl transpeptidase from kidney, Meth. Enzymol. 113 (1985) 400-419.
30. Wilbey R.A., Estimating the degree of heat treatment given to milk, J. Soc. Dairy Technol. 49 (1996) 109-112.
31. Zehetner G., Bareuther C., Henle T., Klostermeyer H., Inactivation kinetics of γ-glutamyl-transferase during the heating of milk, Z. Lebensm. Unters. Forsch. 201 (1995) 336-338.