Work

Construction and application of a bifunctional enzyme for the simultaneous enzymatic transformation of zearalenone and deoxynivalenol

Year: 2025

Type: article

Abstract: Zearalenone (ZEN) and deoxynivalenol (DON) are two common toxins that often coexist and observed simultaneously in foods. In this study, we constructed and characterized the fusion enzymes consisting of ZEN lactonase (ZENM) from Monosporascus sp. GIB2. and DON dehydrogenase ( Pe DDH) from Pelagibacterium sp. SCN 63–126. The arrangement of protein domains, as well as the type and length of linker peptides were optimized for the fusion protein. When Pe DDH was positioned at the N-terminus of the fusion enzyme, the utilization of rigid linker peptides (EAAAK) 2 and (EAAAK) 3 led to a 70 % enhancement in the transformation activity of DON compared to flexible linkers (GGGGS) 2 and (GGGGS) 3 . Additionally, the longer linkers (EAAAK) 2 and (EAAAK) 3 enhanced DON transformation by approximately 70 % compared to EAAAK alone. Among all fusion constructed with different enzyme orders, the enzymatic transformation rate of ZEN exceeded 75 %, while positioning Pe DDH at the forefront of the fusion protein increased DON transformation from 68 % to 98 %. Following exploration of the reaction conditions, the fusion protein Pe DDH-(EAAAK) 3 -ZENM achieved an enzymatic transformation rate of 100 % for DON (30 μg/mL) within 16 h and 100 % for ZEN (80 μg/mL) within 30 min, indicating a great potential for the simultaneous transformation of ZEN and DON.

Source: International Journal of Biological Macromolecules

DOI: 10.1016/j.ijbiomac.2025.146534

Authors: Jiayi Yao, Binbin Ouyang, Dawei Ni, Wei Xu, Wenli Zhang, Wanmeng Mu

Institutions: Jiangnan University, State Key Laboratory of Food Science and Technology

Language: English

Topic: Mycotoxins in Agriculture and Food

Subfield: Plant Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

SDG: Zero hunger

Open Access status: hybrid

Estimated APC paid: $4,390