| Full text | |
| Author(s): |
Goncalves Dias, Fernanda Furlan
;
Bogusz Junior, Stanislau
;
Hantao, Leandro Wang
;
Augusto, Fabio
;
Sato, Helia Harumi
Total Authors: 5
|
| Document type: | Journal article |
| Source: | LWT-FOOD SCIENCE AND TECHNOLOGY; v. 76, n. B, SI, p. 222-229, MAR 2017. |
| Web of Science Citations: | 0 |
| Abstract | |
The Maillard reaction is responsible for color and flavor formation in fried, roasted and baked foods. However, this reaction can also promote the formation of acrylamide, a potential human carcinogen. The application of L-asparaginase represents a promising method for acrylamide mitigation in heated products by the direct conversion of the precursor L-asparagine to L-aspartic acid and ammonia, which does not lead to additional acrylamide formation. Our research group produced and purified an L-asparaginase from native Aspergillus oryzae CCT 3940 with highly potential for acrylamide mitigation. To verify the enzymatic effectiveness, we compared the native L-asparaginase with the commercial recombinant enzyme. For this purpose, a GC-MS/MS method was developed, optimized and validated for the assessment of acrylamide in French fries. Our results indicate a relationship between the L-asparagine content and acrylamide formation in French fries. The acrylamide concentration of the fried potato treated with the L-asparaginase from A. oryzae CCT 3940 and treated with commercial enzyme reduced 72% and 92%, respectively compared to control sample. Moreover, the L-asparaginase from A. oryzae CCT 3940 showed no L-glutaminase activity, while commercial enzyme promoted a decrease in the L-glutamine content (25%). Our results suggest that L-asparaginase from A. oryzae CCT 3940 may be of great value for acrylamide mitigation. (C) 2016 Elsevier Ltd. All rights reserved. (AU) | |
| FAPESP's process: | 12/24046-7 - Production, biochemical characterization and application of fungal L-asparaginase |
| Grantee: | Hélia Harumi Sato |
| Support Opportunities: | Regular Research Grants |