Enzyme Technology for Detoxification of Mycotoxins in Animal Feed

Moll, Wulf-Dieter

doi:10.1002/9783527813780.ch3_2

Cited by 5 publications

(6 citation statements)

References 170 publications

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“…A potential application other than gastrointestinal detoxification of ZEN with a recombinant feed enzyme could be to express zenA in genetically modified crop plants for in planta hydrolytic degradation of ZEN. However, ZEN degradation may not convey much resistance against Fusarium infection, and harvested cereal grain could still be contaminated with deoxynivalenol.…”

Section: Discussionmentioning

confidence: 99%

“…A possible mitigation strategy for the xenoestrogenic activity of ZEN in animals would be the use of an enzyme as a feed additive for the gastrointestinal conversion of ZEN to nonestrogenic reaction products. Such an approach has been successfully implemented with fumonisin esterase for hydrolytic detoxification of fumonisins. − ZEN has a lactone ester bond, which is also susceptible to hydrolytic cleavage (Scheme ). 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 ().…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

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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“…The recombinant carboxylesterase (18 U/L) was shown to completely convert 60 μg/mL of FB1 to HFB1 after a 15 min co-incubation at 30 °C and pH 8.0 [ 144 ] completely degraded 4.63 μM FB1 to HFB1 within 15 min at 30 °C. The enzyme was commercialized by the BIOMIN company as FUMzyme ® and successfully authorized by EU for use as a feed additive enabling gastrointestinal deesterification of FB1 in pigs and poultry [ 145 ]. Further studies of this preparation confirmed its high efficiency as a feed additive in pigs, turkeys, and chickens [ 146 ] as well as a significant (>80%) reduction of the FB content in the maize grain after a 1 h treatment [ 147 ].…”

Section: Biotransformation Of Fumonisin B1mentioning

confidence: 99%

Post-Harvest Prevention of Fusariotoxin Contamination of Agricultural Products by Irreversible Microbial Biotransformation: Current Status and Prospects

Statsyuk

Popletaeva

Щербакова

2023

BioTech

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Biological degradation of mycotoxins is a promising environmentally-friendly alternative to chemical and physical detoxification methods. To date, a lot of microorganisms able to degrade them have been described; however, the number of studies determining degradation mechanisms and irreversibility of transformation, identifying resulting metabolites, and evaluating in vivo efficiency and safety of such biodegradation is significantly lower. At the same time, these data are crucial for the evaluation of the potential of the practical application of such microorganisms as mycotoxin-decontaminating agents or sources of mycotoxin-degrading enzymes. To date, there are no published reviews, which would be focused only on mycotoxin-degrading microorganisms with the proved irreversible transformation of these compounds into less toxic compounds. In this review, the existing information about microorganisms able to efficiently transform the three most common fusariotoxins (zearalenone, deoxinyvalenol, and fumonisin B1) is presented with allowance for the data on the corresponding irreversible transformation pathways, produced metabolites, and/or toxicity reduction. The recent data on the enzymes responsible for the irreversible transformation of these fusariotoxins are also presented, and the promising future trends in the studies in this area are discussed.

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“…27 Eubacterium BBSH797 and Trichosporon mycotoxinivorans were the first microorganisms used for mycotoxin biotransformation. 28 The substrate is known as a substance that is modified by an enzyme. A transient enzyme−substrate complex is formed during the biotransformation of the substrate by enzymes.…”

Section: Biotransformation Of Mycotoxins and The Mechanisms Of Action...mentioning

confidence: 99%

Microbial Enzymes Involved in the Biotransformation of Major Mycotoxins

Adegoke

Yang

Xing

et al. 2022

J. Agric. Food Chem.

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Mycotoxins, the most researched biological toxins, can contaminate food and feed, resulting in severe health implications for humans and animals. Physical, chemical, and biological techniques are used to mitigate mycotoxin contamination. The biotransformation method using whole microbial cells or isolated enzymes is the best choice to mitigate mycotoxins. Using specific enzymes may avoid the disadvantages of utilizing a full microbe, such as accidental harm to the product's organoleptic characteristics and hazardous safety features. Moreover, the degradation rates of the isolated enzymes are higher than those of the whole-cell reactions, and they are substrate-specific. Their specificity is comprehensive and is shown at the positional and/or chiral center in many circumstances. Currently, only a few enzymes of microbial origin are commercially available. Therefore, there is a need to identify more novel enzymes of microbial origin that can mitigate mycotoxins. In this review, we conducted an in-depth summary of the microbial enzymes involved in the biotransformation of mycotoxins.

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Enzyme Technology for Detoxification of Mycotoxins in Animal Feed

Cited by 5 publications

References 170 publications

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

Bacterial Lactonases ZenA with Noncanonical Structural Features Hydrolyze the Mycotoxin Zearalenone

Post-Harvest Prevention of Fusariotoxin Contamination of Agricultural Products by Irreversible Microbial Biotransformation: Current Status and Prospects

Microbial Enzymes Involved in the Biotransformation of Major Mycotoxins

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