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1.
Article in English | MEDLINE | ID: mdl-18569004

ABSTRACT

Exposure of the Belgian consumer to pesticide residues from the consumption of fruit and vegetables was determined based on data collected in the Belgian food consumption survey performed by the Scientific Institute for Public Health and data from the Belgian Federal Agency for the Safety of the Food Chain 2005 monitoring programme. A first screening of pesticide residue exposure was performed by a deterministic approach. For most pesticide residues studied, the exposure was 100 times lower than the acceptable daily intake (ADI). However, for a high consumer (97.5th percentile of consumption) the intake could reach 23% of the ADI for imazalil, 15% for chlorpropham, 14% for the dithiocarbamates, 10% for dimethoate and lambda-cyhalothrin, and 9% for chlorpyriphos. Nevertheless, probabilistic exposure assessment performed on these pesticides in a second phase of the study indicated that, except for chlorpropham, the probability to exceed the ADI is much lower than 0.1%.


Subject(s)
Food Contamination/analysis , Fruit/chemistry , Pesticide Residues/analysis , Vegetables/chemistry , Belgium , Maximum Allowable Concentration , Models, Biological , Risk Assessment/statistics & numerical data , Statistics as Topic
2.
J Dairy Res ; 68(2): 287-301, 2001 May.
Article in English | MEDLINE | ID: mdl-11504392

ABSTRACT

A detailed kinetic study of hydroxymethylfurfural, lactulose and furosine formation was performed upon heating milk at temperatures between 90 degrees C and 140 degrees C. In case of prolonged heating, formation kinetics could be described by a fractional conversion model. Considering only the first phase of the model, kinetics could be simplified to a pseudo-zero order model. A first assessment of kinetic parameters was made by isothermal experiments. Data were analysed using both a 2-step linear and a 1-step non-linear regression method. Only for furosine, did the global 1-step regression approach seem to give better results than the individual 2-step regression approach. Next, the estimated parameters k(ref) and Ea were re-evaluated under non-isothermal conditions by subjecting milk to a time variable temperature profile. Given the complexity of Maillard reaction, it seemed better to estimate kinetic parameters under non-isothermal conditions when using a simplified model. Formation of hydroxymethylfurfural, lactulose and furosine was characterized by an Ea value of 90.2 kJ/mol (k(110 degrees C) = 1.2 micromol/l, min), 99.1 kJ/mol (k(110 degrees C) = 51.5 mg/l, min) and 88.7 kJ/mol (k(110 degrees C) = 16.3 mg/100 g protein, min) respectively. Additionally, 90% joint confidence regions were constructed in order to obtain an accurate representation of the statistical confidence associated with the simultaneously estimated parameters.


Subject(s)
Furaldehyde/analogs & derivatives , Furaldehyde/chemical synthesis , Lactulose/chemical synthesis , Lysine/analogs & derivatives , Lysine/chemical synthesis , Milk/chemistry , Animals , Cattle , Gastrointestinal Agents/chemistry , Hot Temperature , Kinetics , Models, Chemical , Regression Analysis , Thermodynamics
3.
J Dairy Res ; 68(1): 95-107, 2001 Feb.
Article in English | MEDLINE | ID: mdl-11289274

ABSTRACT

A detailed kinetic study of alkaline phosphatase, lactoperoxidase and beta-lactoglobulin was carried out in the context of identifying intrinsic time-temperature indicators for controlling the heat processing of milk. The heat inactivation or denaturation of alkaline phosphatase, lactoperoxidase and beta-lactoglobulin under isothermal conditions was found to follow first order kinetics. Experimental results were analysed using both a two step linear regression and a one step non-linear regression method. Results obtained using the two statistical techniques were comparable, but the 95% confidence interval for the predicted values was smaller when the one step non-linear regression method was used, indicating its superiority for estimating kinetic parameters. Thermal inactivation of alkaline phosphatase and lactoperoxidase was characterized by z values of 5.3 deg C (D60 degrees C = 24.6 min) and 4.3 deg C (D71 degrees C = 38.6 min) respectively. For the denaturation of beta-lactoglobulin we found z values of 7.9 deg C (D7.5 degrees C = 49.9 min) in the temperature range 70-80 degrees C and 24.2 deg C (D85 degrees C = 3.53 min) in the range 83-95 degrees C. Dref and z were evaluated under dynamic temperature conditions. To estimate the statistical accuracy of the parameters, 90% joint confidence regions were constructed.


Subject(s)
Alkaline Phosphatase/metabolism , Hot Temperature , Lactoglobulins/metabolism , Lactoperoxidase/metabolism , Milk/enzymology , Animals , Cattle , Kinetics , Linear Models , Milk/metabolism , Protein Denaturation
4.
J Dairy Res ; 68(4): 625-37, 2001 Nov.
Article in English | MEDLINE | ID: mdl-11928959

ABSTRACT

At atmospheric pressure, inactivation of lactoperoxidase (LPO) in milk and whey was studied in a temperature range of 69-73 degrees C and followed first order kinetics. Temperature dependence of the first order inactivation rate constants could be accurately described by the Arrhenius equation, with an activation energy of 635.3 +/- 70.7 kJ/mol for raw bovine milk and 736.9 +/- 40.9 kJ/mol for diluted whey, indicating a very high temperature sensitivity. On the other hand, LPO is very pressure resistant and not or only slightly affected by treatment at pressure up to 700 MPa combined with temperatures between 20 and 65 degrees C. Both for thermal and pressure treatment, stability of LPO was higher in milk than in diluted whey. Besides, a very pronounced antagonistic effect between high temperature and pressure was observed, i.e. at 73 degrees C, a temperature where thermal inactivation at atmospheric pressure occurs rapidly, application of pressure up to 700 MPa exerted a protective effect. At atmospheric pressure, LPO in diluted whey was optimally active at a temperature of about 50 degrees C. At all temperatures studied (20-60 degrees C), LPO remained active during pressure treatment up to 300 MPa, although the activity was significantly reduced at pressures higher than 100 MPa. The optimal temperature was found to shift to lower values (30-40 degrees C) with increasing pressure.


Subject(s)
Lactoperoxidase/metabolism , Milk Proteins/metabolism , Milk/enzymology , Pressure , Temperature , Animals , Cattle , Enzyme Activation , Enzyme Stability , Kinetics , Thermodynamics , Whey Proteins
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