Zearalenone lactonase: characteristics, modification, and application

Fang, Yuanyuan; Zhang, Zhenxia; Xu, Wei; Zhang, Wenli; Guang, Cuie; Mu, Wanmeng

doi:10.1007/s00253-022-12205-5

Cited by 15 publications

(9 citation statements)

References 42 publications

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“…ZENY was stable at 35 °C and below and retained approximately 70 and 40% of its activity at 40 and 50 °C, respectively. These findings are consistent with the behavior of most reported hydrolases, underscoring the typical nature of ZENY’s activity.…”

Section: Resultsmentioning

confidence: 99%

Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis

Shi,

Mwabulili,

Xie

et al. 2024

J. Agric. Food Chem.

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Zearalenone (ZEN) is a widespread mycotoxin that causes serious damage to animal husbandry and poses a threat to human health. A screen of ZEN-degrading soil bacteria yielded Bacillus subtilis YT-4, which yielded 80% ZEN degradation after 6 h and 95% after 36 h. The gene sequence encoding the degradative enzyme ZENY was mined from the genome of YT-4 and expressed in yeast. ZENY is an α/β-hydrolase with an optimal enzyme activity at 37 °C and pH 8. By breaking the lactone ring of ZEN, it produces ZENY-C 18 H 24 O 5 with a molecular weight of 320.16 g/mol. Sequence comparison and molecular docking analyses identified the catalytic ZENY triad 99S-245H-123E and the primary ZEN-binding mode within the hydrophobic pocket of the enzyme. To improve the thermal stability of the enzyme for industrial applications, we introduced a mutation at the N-terminus, specifically replacing the fifth residue N with V, and achieved a 25% improvement in stability at 45 °C. These findings aim to achieve ZEN biodegradation and provide insight into the structure and function of ZEN hydrolases.

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Section: Resultsmentioning

confidence: 99%

Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis

Shi,

Mwabulili,

Xie

et al. 2024

J. Agric. Food Chem.

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“…This interest is due to a possible increase in the level of food safety for humans and animals arising from their consumption of food and feeds contaminated with mycotoxins, respectively, due to their detoxification under mild conditions as a result of the action of various enzymatic catalysts [ 74 , 75 , 76 ]. It is already known today that lactonases may be among such potentially effective destructors [ 76 , 77 , 78 ], since individual mycotoxins contain lactone structures similar to AHLs in their structures. Since His 6 -OPH is active in relation to AHLs and catalyzes their hydrolysis similarly to well-known lactonases, this determines the interest in the enzyme under discussion as a possible destructor of not only AHLs but also mycotoxins with corresponding chemical structures.…”

Section: Stabilized and Immobilized His-tagged Oph In The Hydrolysis ...mentioning

confidence: 99%

“…It should be noted that the use of immobilized forms of lactonases is considered promising since they provide high stability during storage and in catalytic treatments of various objects contaminated with mycotoxins [ 76 , 78 , 79 ].…”

Section: Stabilized and Immobilized His-tagged Oph In The Hydrolysis ...mentioning

confidence: 99%

Carrier Variety Used in Immobilization of His6-OPH Extends Its Application Areas

et al. 2023

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Organophosphorus hydrolase, containing a genetically introduced hexahistidine sequence (His6-OPH), attracts the attention of researchers by its promiscuous activity in hydrolytic reactions with various substrates, such as organophosphorus pesticides and chemical warfare agents, mycotoxins, and N-acyl homoserine lactones. The application of various carrier materials (metal-organic frameworks, polypeptides, bacterial cellulose, polyhydroxybutyrate, succinylated gelatin, etc.) for the immobilization and stabilization of His6-OPH by various methods, enables creation of biocatalysts with various properties and potential uses, in particular, as antidotes, recognition elements of biosensors, in fibers with chemical and biological protection, dressings with antimicrobial properties, highly porous sorbents for the degradation of toxicants, including in flow systems, etc. The use of computer modeling methods in the development of immobilized His6-OPH samples provides in silico prediction of emerging interactions between the enzyme and immobilizing polymer, which may have negative effects on the catalytic properties of the enzyme, and selection of the best options for experiments in vitro and in vivo. This review is aimed at analysis of known developments with immobilized His6-OPH, which allows to recognize existing recent trends in this field of research, as well as to identify the reasons limiting the use of a number of polymer molecules for the immobilization of this enzyme.

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“…A hydrolase with specificity for ZEN was found to be produced by Clonostachys rosea , and the enzyme, ZHD101, was identified and characterized, including its X-ray crystal structure determination. , The enzymatic reaction has a preliminary EC number 3.1.1.B12 (). Orthologs are harbored by several other fungi, , and activities, kinetic parameters, and crystal structures were determined for some of these sequences. − The primary product of enzymatic hydrolysis has long escaped detection because it is too hydrophilic to partition into an organic solvent and was consequently missed when organic extracts were analyzed . Following the logic of recommended abbreviations for ZEN and derivates, we use the abbreviation HZEN for the nonestrogenic hydrolyzed zearalenone and DHZEN for the previously reported, also nonestrogenic secondary reaction product decarboxylated hydrolyzed zearalenone (Scheme ).…”

Section: Introductionmentioning

confidence: 99%

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

Fruhauf,

Pühringer,

Thamhesl

et al. 2024

ACS Catal.

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Zearalenone (ZEN) is a mycoestrogenic polyketide produced by Fusarium graminearum and other phytopathogenic members of the genus Fusarium. Contamination of cereals with ZEN is frequent, and hydrolytic detoxification with fungal lactonases has been explored. Here, we report the isolation of a bacterial strain, Rhodococcus erythropolis PFA D8−1, with ZEN hydrolyzing activity, cloning of the gene encoding α/β hydrolase ZenA encoded on the linear megaplasmid pSFRL1, and biochemical characterization of nine homologues. Furthermore, we report sitedirected mutagenesis as well as structural analysis of the dimeric ZenA Re of R. erythropolis and the more thermostable, tetrameric ZenA Scfl of Streptomyces coelicoflavus with and without bound ligands. The X-ray crystal structures not only revealed canonical features of α/β hydrolases with a cap domain including a Ser-His-Asp catalytic triad but also unusual features including an uncommon oxyanion hole motif and a peripheral, short antiparallel β-sheet involved in tetramer interactions. Presteady-state kinetic analyses for ZenA Re and ZenA Scfl identified balanced rate-limiting steps of the reaction cycle, which can change depending on temperature. Some new bacterial ZEN lactonases have lower K M and higher k cat than the known fungal ZEN lactonases and may lend themselves to enzyme technology development for the degradation of ZEN in feed or food.

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Zearalenone lactonase: characteristics, modification, and application

Cited by 15 publications

References 42 publications

Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis

Characterization, Structural Analysis, and Thermal Stability Mutation of a New Zearalenone-Degrading Enzyme Mined from Bacillus subtilis

Carrier Variety Used in Immobilization of His6-OPH Extends Its Application Areas

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

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