A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101
Deoxynivalenol (DON), primarily generated by <i>Fusarium</i> species, often exists in agricultural products. It can be transformed to 3-<i>epi</i>-deoxynivalenol (3-<i>epi</i>-DON), with a relatively low toxicity, via two steps. DDH in <i>Pelagibacterium hal...
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MDPI AG
2024-03-01
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author | Yanrong Liu Mingxin Ma Yu Tang Zhenqian Huang Yongpeng Guo Qiugang Ma Lihong Zhao |
author_facet | Yanrong Liu Mingxin Ma Yu Tang Zhenqian Huang Yongpeng Guo Qiugang Ma Lihong Zhao |
author_sort | Yanrong Liu |
collection | DOAJ |
description | Deoxynivalenol (DON), primarily generated by <i>Fusarium</i> species, often exists in agricultural products. It can be transformed to 3-<i>epi</i>-deoxynivalenol (3-<i>epi</i>-DON), with a relatively low toxicity, via two steps. DDH in <i>Pelagibacterium halotolerans</i> ANSP101 was proved to convert DON to 3-keto-deoxynivalenol (3-keto-DON). In the present research, AKR4, a NADPH-dependent aldo/keto reductase from <i>P. halotolerans</i> ANSP101, was identified to be capable of converting 3-keto-DON into 3-<i>epi</i>-DON. Our results demonstrated that AKR4 is clearly a NADPH-dependent enzyme, for its utilization of NADPH is higher than that of NADH. AKR4 functions at a range of pH 5–10 and temperatures of 20–60 °C. AKR4 is able to degrade 89% of 3-keto-DON in 90 min at pH 7 and 50 °C with NADPH as the cofactor. The discovery of AKR4, serving as an enzyme involved in the final step in DON degradation, might provide an option for the final detoxification of DON in food and feed. |
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spelling | doaj.art-248d8174e95c4ea7a25008ad1e61599b2024-04-12T13:18:35ZengMDPI AGFoods2304-81582024-03-01137106410.3390/foods13071064A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101Yanrong Liu0Mingxin Ma1Yu Tang2Zhenqian Huang3Yongpeng Guo4Qiugang Ma5Lihong Zhao6State Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaCollege of Animal Science and Technology, Henan Agricultural University, Zhengzhou 450046, ChinaState Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaState Key Laboratory of Animal Nutrition and Feeding, Poultry Nutrition and Feed Technology Innovation Team, College of Animal Science and Technology, China Agricultural University, Beijing 100193, ChinaDeoxynivalenol (DON), primarily generated by <i>Fusarium</i> species, often exists in agricultural products. It can be transformed to 3-<i>epi</i>-deoxynivalenol (3-<i>epi</i>-DON), with a relatively low toxicity, via two steps. DDH in <i>Pelagibacterium halotolerans</i> ANSP101 was proved to convert DON to 3-keto-deoxynivalenol (3-keto-DON). In the present research, AKR4, a NADPH-dependent aldo/keto reductase from <i>P. halotolerans</i> ANSP101, was identified to be capable of converting 3-keto-DON into 3-<i>epi</i>-DON. Our results demonstrated that AKR4 is clearly a NADPH-dependent enzyme, for its utilization of NADPH is higher than that of NADH. AKR4 functions at a range of pH 5–10 and temperatures of 20–60 °C. AKR4 is able to degrade 89% of 3-keto-DON in 90 min at pH 7 and 50 °C with NADPH as the cofactor. The discovery of AKR4, serving as an enzyme involved in the final step in DON degradation, might provide an option for the final detoxification of DON in food and feed.https://www.mdpi.com/2304-8158/13/7/1064Deoxynivalenol (DON)3-keto-DON3-<i>epi</i>-DONaldo/keto reductasebiodegradation |
spellingShingle | Yanrong Liu Mingxin Ma Yu Tang Zhenqian Huang Yongpeng Guo Qiugang Ma Lihong Zhao A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 Foods Deoxynivalenol (DON) 3-keto-DON 3-<i>epi</i>-DON aldo/keto reductase biodegradation |
title | A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 |
title_full | A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 |
title_fullStr | A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 |
title_full_unstemmed | A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 |
title_short | A NADPH-Dependent Aldo/Keto Reductase Is Responsible for Detoxifying 3-Keto-Deoxynivalenol to 3-<i>epi</i>-Deoxynivalenol in <i>Pelagibacterium halotolerans</i> ANSP101 |
title_sort | nadph dependent aldo keto reductase is responsible for detoxifying 3 keto deoxynivalenol to 3 i epi i deoxynivalenol in i pelagibacterium halotolerans i ansp101 |
topic | Deoxynivalenol (DON) 3-keto-DON 3-<i>epi</i>-DON aldo/keto reductase biodegradation |
url | https://www.mdpi.com/2304-8158/13/7/1064 |
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