22.12.2012 Views

3. FOOD ChEMISTRy & bIOTEChNOLOGy 3.1. Lectures

3. FOOD ChEMISTRy & bIOTEChNOLOGy 3.1. Lectures

3. FOOD ChEMISTRy & bIOTEChNOLOGy 3.1. Lectures

SHOW MORE
SHOW LESS

Create successful ePaper yourself

Turn your PDF publications into a flip-book with our unique Google optimized e-Paper software.

Chem. Listy, 102, s265–s1311 (2008) Food Chemistry & Biotechnology<br />

these kinds of products such as darkness, yellowness, appearance,<br />

stickiness, crispness, oiliness, flavour, off-flavour, saltiness,<br />

sweetness and overall acceptability. Changes in colour<br />

were observed in pancakes prepared under different heating<br />

programmes, where darkness and crispness were more intensive<br />

in pancakes prepared at higher temperature of frying.<br />

no differences in evaluated sensory properties mentioned<br />

above were found out in any case of L-asparaginase application<br />

(P = 99 %) that was consider as a great advantage of<br />

the presented effective way of acrylamide reduction in food<br />

products 24 .<br />

AA (ng/g FW) .<br />

700<br />

600<br />

500<br />

400<br />

300<br />

200<br />

100<br />

0<br />

without enzyme<br />

2 U/g FW of enzyme; 10 min/ 37 °C incubation<br />

10 U/g FW of enzyme; 10 min/ 37 °C incubation<br />

Marabel Bellarosa<br />

Fig. <strong>3.</strong> Amount of acrylamide (AA) in raw potatoes (varieties<br />

Marabel and bellarosa) after enzymatic treatment (L-asparaginase<br />

produced by A. oryzae applied at concentration of 2 and<br />

10 u g –1 Fw and incubated at 37 °C for 10 min) and following<br />

heat treatment at 180 °C for 20 min<br />

AA (ug/kg FW) .<br />

800<br />

700<br />

600<br />

500<br />

400<br />

300<br />

200<br />

100<br />

0<br />

without enzyme 1 U/g FW of enzyme, 30 min/ 37°C incubation<br />

175 °C/20 min 180 °C/20 min 200 °C/20 min<br />

Fig. 4. Amount of acrylamide (AA) in pancakes prepared from<br />

potato-wheat powder at different heating temperatures (175 °C,<br />

180 °C and 200 °C) for 20 min with previous enzymatic treatment<br />

(L-asparaginase produced by A. oryzae applied at concentration<br />

of 1 u g –1 Fw and incubated at 37 °C for 30 min)<br />

Conclusions<br />

Since the acrylamide occurrence in foods and its potentiality<br />

to cause detrimental affects on human health attracts<br />

attention in all over the word, the effort to minimize its level<br />

in foods and consequently the human exposure to acrylamide<br />

is extremely advisable. Among many ways of acrylamide reduction<br />

the application of enzyme in order to prevent acry-<br />

s542<br />

lamide formation is feasible and effective without any undesirable<br />

effect on sensory quality of final products. For that<br />

reason, this procedure is protected by the patent application<br />

filed with the Industrial Property Office of the Slovak Republic<br />

under the number 5027-2006.<br />

This work was supported by the Slovak Research and<br />

Development Agency under the contract No. COST-0015-06.<br />

REFEREnCES<br />

1. Tareke E., Rydberg P., Karlsson P., Eriksson S., Tornqvist<br />

M.: J. Agric. Food Chem. 50, 4998 (2002).<br />

2. JECFA 2005 64th meeting Rome, 8-17 February 2005:<br />

http://www.who.int/ipcs/food/jecfa/summaries/summary_report_64_final.pdf<br />

<strong>3.</strong> IARC. Acrylamide. In IARC Monographs on the evaluation<br />

of carcinogen risk to humans: some industrial<br />

chemicals. International Agency for Research on Cancer,<br />

60, p. 389, Lyon, France 1994.<br />

4. Commission Recommendation of 3 May 2007 on the<br />

monitoring of acrylamide levels in food (notified under<br />

document number C(2007) 1873).<br />

5. Hogervorst J. G., Schouten L. J., Konings E. J.,<br />

Goldbohm R. A., Van Den Brandt P. A.: Cancer Epidemiol.<br />

Biomarkers Prevent. 16, 2304 (2008).<br />

6. Olesen P. T., Olsen A., Frandsen H., Frederiksen K.,<br />

Overvad K., Tjonneland A.: Int. J. Canc. 122, 2094<br />

(2008).<br />

7. FAO/WHO (2002): Opinion of the Scientific Committee<br />

on Food on new findings regarding the presence of acrylamide<br />

in food, Brussels, 3 July 2002.<br />

8. Mottram D. S., Wedzicha B. L., Dodson A. T.: nature<br />

419, 448 (2002).<br />

9. Stadler R. H., Blank I., Varga n., Robert F., Hau J.,<br />

Guy P. A., Robert M. C., Riediker S.: nature 419, 449<br />

(2002).<br />

10. Zyzak D. V., Sanders R .A., Stojanovic M., Tallmadge<br />

D. H., Eberhart B. L., Ewald D. K., Gruber D. C., Morsch<br />

T. R., Strothers M. A., Rizzi G. P., Villagran M. D.:<br />

J. Agric. Food Chem. 51, 4782 (2003).<br />

11. Yaylayan V. A., Wnorowski, A., Perez-Locas C.: J. Agric.<br />

Food Chem. 51, 1753 (2003).<br />

12. Biedermann M., Grob K.: Mitt. Geb. Lebensmitt. Hyg.<br />

94, 406 (2003).<br />

1<strong>3.</strong> Ciesarová Z., Kiss E., Kolek, E.: Czech J. Food Sci. 24,<br />

133 (2006).<br />

14. CIAA Acrylamide Toolbox [on-line]. Brussels : Confederation<br />

of the Food and Drink Industries of the European<br />

Union, 11 December 2007.<br />

15. Ciesarová Z.: Chem. Listy 99, 483 (2005).<br />

16. Kolek E., Šimon P., Šimko P.: J. Food Sci. 72, E341<br />

(2007).<br />

17. Kolek E., Šimko P., Šimon P., Gatial, A.: J. Food nutr.<br />

Res. 46, 39 (2007).<br />

19. Senyuva H. Z., Gökmen V.: Food Add. Contam. 22, 214<br />

(2005).

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!