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Journal articles on the topic 'Detoxification enzymes'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Barrett, J. "Helminth detoxification mechanisms." Journal of Helminthology 71, no. 2 (June 1997): 85–90. http://dx.doi.org/10.1017/s0022149x0001573x.

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Detoxification mechanisms in parasitic helminths have not been extensively studied, despite their obvious relevance to drug development and drug resistance. Differences in detoxification enzymes between the parasite and its host may be exploitable in the design of pro-drugs, whilst selective inhibition of the parasites protective enzymes could increase their sensitivity to drug action and also make them more susceptible to the host's defence mechanisms.

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2

Guan, Yun, Jia Chen, Eugenie Nepovimova, Miao Long, Wenda Wu, and Kamil Kuca. "Aflatoxin Detoxification Using Microorganisms and Enzymes." Toxins 13, no. 1 (January 9, 2021): 46. http://dx.doi.org/10.3390/toxins13010046.

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Mycotoxin contamination causes significant economic loss to food and feed industries and seriously threatens human health. Aflatoxins (AFs) are one of the most harmful mycotoxins, which are produced by Aspergillus flavus, Aspergillus parasiticus, and other fungi that are commonly found in the production and preservation of grain and feed. AFs can cause harm to animal and human health due to their toxic (carcinogenic, teratogenic, and mutagenic) effects. How to remove AF has become a major problem: biological methods cause no contamination, have high specificity, and work at high temperature, affording environmental protection. In the present research, microorganisms with detoxification effects researched in recent years are reviewed, the detoxification mechanism of microbes on AFs, the safety of degrading enzymes and reaction products formed in the degradation process, and the application of microorganisms as detoxification strategies for AFs were investigated. One of the main aims of the work is to provide a reliable reference strategy for biological detoxification of AFs.

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3

Guan, Yun, Jia Chen, Eugenie Nepovimova, Miao Long, Wenda Wu, and Kamil Kuca. "Aflatoxin Detoxification Using Microorganisms and Enzymes." Toxins 13, no. 1 (January 9, 2021): 46. http://dx.doi.org/10.3390/toxins13010046.

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Mycotoxin contamination causes significant economic loss to food and feed industries and seriously threatens human health. Aflatoxins (AFs) are one of the most harmful mycotoxins, which are produced by Aspergillus flavus, Aspergillus parasiticus, and other fungi that are commonly found in the production and preservation of grain and feed. AFs can cause harm to animal and human health due to their toxic (carcinogenic, teratogenic, and mutagenic) effects. How to remove AF has become a major problem: biological methods cause no contamination, have high specificity, and work at high temperature, affording environmental protection. In the present research, microorganisms with detoxification effects researched in recent years are reviewed, the detoxification mechanism of microbes on AFs, the safety of degrading enzymes and reaction products formed in the degradation process, and the application of microorganisms as detoxification strategies for AFs were investigated. One of the main aims of the work is to provide a reliable reference strategy for biological detoxification of AFs.

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4

Cohen, Martin R., C. N. Ramchand, Voyta Sailer, Maria Fernandez, William McAmis, N. Sridhara, and Cornelius Alston. "Detoxification enzymes following intrastriatal kainic acid." Neurochemical Research 12, no. 5 (May 1987): 425–29. http://dx.doi.org/10.1007/bf00972293.

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5

Lyagin, Ilya, and Elena Efremenko. "Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action." Molecules 24, no. 13 (June 26, 2019): 2362. http://dx.doi.org/10.3390/molecules24132362.

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Mycotoxins are highly dangerous natural compounds produced by various fungi. Enzymatic transformation seems to be the most promising method for detoxification of mycotoxins. This review summarizes current information on enzymes of different classes to convert various mycotoxins. An in-depth analysis of 11 key enzyme mechanisms towards dozens of major mycotoxins was realized. Additionally, molecular docking of mycotoxins to enzymes’ active centers was carried out to clarify some of these catalytic mechanisms. Analyzing protein homologues from various organisms (plants, animals, fungi, and bacteria), the prevalence and availability of natural sources of active biocatalysts with a high practical potential is discussed. The importance of multifunctional enzyme combinations for detoxification of mycotoxins is posed.

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6

Kotze, Andrew C., Angela P. Ruffell, and Aaron B. Ingham. "Phenobarbital Induction and Chemical Synergism Demonstrate the Role of UDP-Glucuronosyltransferases in Detoxification of Naphthalophos by Haemonchus contortus Larvae." Antimicrobial Agents and Chemotherapy 58, no. 12 (October 6, 2014): 7475–83. http://dx.doi.org/10.1128/aac.03333-14.

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ABSTRACTWe used an enzyme induction approach to study the role of detoxification enzymes in the interaction of the anthelmintic compound naphthalophos withHaemonchus contortuslarvae. Larvae were treated with the barbiturate phenobarbital, which is known to induce the activity of a number of detoxification enzymes in mammals and insects, including cytochromes P450 (CYPs), UDP-glucuronosyltransferases (UDPGTs), and glutathione (GSH)S-transferases (GSTs). Cotreatment of larvae with phenobarbital and naphthalophos resulted in a significant increase in the naphthalophos 50% inhibitory concentration (IC50) compared to treatment of larvae with the anthelmintic alone (up to a 28-fold increase). The phenobarbital-induced drug tolerance was reversed by cotreatment with the UDPGT inhibitors 5-nitrouracil, 4,6-dihydroxy-5-nitropyrimidine, probenecid, and sulfinpyrazone. Isobologram analysis of the interaction of 5-nitrouracil with naphthalophos in phenobarbital-treated larvae clearly showed the presence of strong synergism. The UDPGT inhibitors 5-nitrouracil, 4,6-dihydroxy-5-nitropyrimidine, and probenecid also showed synergistic effects with non-phenobarbital-treated worms (synergism ratio up to 3.2-fold). This study indicates thatH. contortuslarvae possess one or more UDPGT enzymes able to detoxify naphthalophos. In highlighting the protective role of this enzyme group, this study reveals the potential for UDPGT enzymes to act as a resistance mechanism that may develop under drug selection pressure in field isolates of this species. In addition, the data indicate the potential for a chemotherapeutic approach utilizing inhibitors of UDPGT enzymes as synergists to increase the activity of naphthalophos against parasitic worms and to combat detoxification-mediated drug resistance if it arises in the field.

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7

Reed, Lindsay, Volker M. Arlt, and David H. Phillips. "The role of cytochrome P450 enzymes in carcinogen activation and detoxication: an in vivo–in vitro paradox." Carcinogenesis 39, no. 7 (May 3, 2018): 851–59. http://dx.doi.org/10.1093/carcin/bgy058.

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Cytochrome P450 enzyme systems have been widely used in vitro to determine the pathways of activation of procarcinogens, but paradoxically, these same enzymes can play a more predominant role in carcinogen detoxification in vivo.

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8

Mahmood, Shahid, Azeem Khalid, Muhammad Arshad, Tariq Mahmood, and David E. Crowley. "Detoxification of azo dyes by bacterial oxidoreductase enzymes." Critical Reviews in Biotechnology 36, no. 4 (February 10, 2015): 639–51. http://dx.doi.org/10.3109/07388551.2015.1004518.

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9

Cornell, H. J., W. Doherty, and T. Stelmasiak. "Papaya latex enzymes capable of detoxification of gliadin." Amino Acids 38, no. 1 (January 21, 2009): 155–65. http://dx.doi.org/10.1007/s00726-008-0223-6.

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10

Belford, Ebenezer J. D., Ulrike Dörfler, Andreas Stampf, and Peter Schröder. "Microsomal Detoxification Enzymes in Yam Bean [Pachyrhizus erosus (L.) Urban]." Zeitschrift für Naturforschung C 59, no. 9-10 (October 1, 2004): 693–700. http://dx.doi.org/10.1515/znc-2004-9-1014.

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Abstract Cytochrome P450s and glutathione-S-transferases (GSTs) constitute two of the largest groups of enzyme families that are responsible for detoxification of exogenous molecules in plants. Their activities differ from plant to plant with respect to metabolism and substrate specificity which is one of the reasons for herbicide selectivity. In the tuber forming yam bean, the legume Pachyrhizus erosus, their activities at the microsomal level were investigated to determine the detoxification status of the plant. The breakdown of the herbicide isoproturon (IPU) to two distinct metabolites, 1-OH-IPU and monodesmethyl-IPU, was demonstrated. GST activity was determined with model substrates, but also by the catalysed formation of the fluorescent glutathione bimane conjugate. This study demonstrates for the first time microsomal detoxification activity in Pachyrhizus and the fluorescence image description of microsomal GST catalysed reaction in a legume.

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11

RAO, R. KOTESWARA, A. SHOBHA RANI, and P. NEERAJA P. NEERAJA. "Ambient Ammonia Stress on Detoxification Enzymes In Brain Tissue of Fish Fingerlings of Cyprinus Carpio." International Journal of Scientific Research 3, no. 1 (June 1, 2012): 491–92. http://dx.doi.org/10.15373/22778179/jan2014/167.

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12

Zhang, Xia, HaiBo Yin, ShiHua Chen, Jun He, and ShanLi Guo. "Changes in Antioxidant Enzyme Activity and Transcript Levels of Related Genes inLimonium sinenseKuntze Seedlings under NaCl Stress." Journal of Chemistry 2014 (2014): 1–6. http://dx.doi.org/10.1155/2014/749047.

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The halophyteLimonium sinenseKuntze is used in traditional Chinese medicine for clearing heat and for detoxification. To examine the detoxification and salt-tolerance mechanisms of this plant, we analyzed antioxidant enzyme activities and transcript levels of genes encoding antioxidant enzymes inL. sinenseseedlings under salt stress (500 mmol/L NaCl). Catalase showed the largest increase in activity, peaking on day 4 of the 7-day NaCl treatment. Peroxidase and superoxide dismutase activities also increased, peaking on days 2 and 3 of the NaCl treatment, respectively. The activities of antioxidant enzymes decreased as the duration of the NaCl treatment extended. The transcript levels of genes encoding antioxidant enzymes were upregulated under NaCl stress. The peak in theLsCATtranscript level was earlier than the peaks inLsAPXandLsGPXtranscript levels. The malondialdehyde content only slightly increased inL. sinenseseedlings under NaCl stress. This was indicative of a low level of lipid peroxidation, consistent with the increased antioxidant enzyme activities and gene transcript levels. These results show that, under NaCl stress, the antioxidant system ofL. sinenseis activated and effectively scavenges reactive oxygen species. This reduces oxidative damage and allows the plant to maintain growth under NaCl stress.

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13

Mills, P. C., D. J. Richardson, J. C. D. Hinton, and S. Spiro. "Detoxification of nitric oxide by the flavorubredoxin of Salmonella enterica serovar Typhimurium." Biochemical Society Transactions 33, no. 1 (February 1, 2005): 198–99. http://dx.doi.org/10.1042/bst0330198.

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Salmonella possesses multiple enzymes that utilize NO as a substrate, and could therefore contribute to the organism's ability to resist nitrosative killing by macrophages. Flavorubredoxin is an oxygen-sensitive enzyme that reduces NO to nitrous oxide. The Salmonella enterica serovar Typhimurium norV gene encoding flavorubredoxin was disrupted and the NO sensitivity of the mutant was determined. The norV mutant showed a greater sensitivity to NO than wild-type S. Typhimurium, but did recover growth after a transient inhibition. The mutant phenotype suggests that multiple enzymes are employed by S. Typhimurium to detoxify NO under anaerobic conditions, one of which is flavorubredoxin.

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14

Hodges, Romilly E., and Deanna M. Minich. "Modulation of Metabolic Detoxification Pathways Using Foods and Food-Derived Components: A Scientific Review with Clinical Application." Journal of Nutrition and Metabolism 2015 (2015): 1–23. http://dx.doi.org/10.1155/2015/760689.

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Research into human biotransformation and elimination systems continues to evolve. Various clinical andin vivostudies have been undertaken to evaluate the effects of foods and food-derived components on the activity of detoxification pathways, including phase I cytochrome P450 enzymes, phase II conjugation enzymes, Nrf2 signaling, and metallothionein. This review summarizes the research in this area to date, highlighting the potential for foods and nutrients to support and/or modulate detoxification functions. Clinical applications to alter detoxification pathway activity and improve patient outcomes are considered, drawing on the growing understanding of the relationship between detoxification functions and different disease states, genetic polymorphisms, and drug-nutrient interactions. Some caution is recommended, however, due to the limitations of current research as well as indications that many nutrients exert biphasic, dose-dependent effects and that genetic polymorphisms may alter outcomes. A whole-foods approach may, therefore, be prudent.

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15

Zhang, Yue-E., Hui-Jing Ma, Dan-Dan Feng, Xiao-Fei Lai, Zhao-Min Chen, Ming-Yue Xu, Quan-You Yu, and Ze Zhang. "Induction of Detoxification Enzymes by Quercetin in the Silkworm." Journal of Economic Entomology 105, no. 3 (June 1, 2012): 1034–42. http://dx.doi.org/10.1603/ec11287.

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16

Wang, Zhiling, Zhong Zhao, Xiaofei Cheng, Suqi Liu, Qin Wei, and Ian M. Scott. "Conifer flavonoid compounds inhibit detoxification enzymes and synergize insecticides." Pesticide Biochemistry and Physiology 127 (February 2016): 1–7. http://dx.doi.org/10.1016/j.pestbp.2015.09.003.

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17

Silva, Marcelo, and Maria da Gloria Carvalho. "Detoxification enzymes: cellular metabolism and susceptibility to various diseases." Revista da Associação Médica Brasileira 64, no. 4 (April 2018): 307–10. http://dx.doi.org/10.1590/1806-9282.64.04.307.

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18

Tomarev, S. I., R. D. Zinovieva, and J. Piatigorsky. "Crystallins of the octopus lens. Recruitment from detoxification enzymes." Journal of Biological Chemistry 266, no. 35 (December 1991): 24226–31. http://dx.doi.org/10.1016/s0021-9258(18)54416-1.

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19

Ben Taheur, Fadia, Bochra Kouidhi, Yasir Mohammed A. Al Qurashi, Jalila Ben Salah-Abbès, and Kamel Chaieb. "Review: Biotechnology of mycotoxins detoxification using microorganisms and enzymes." Toxicon 160 (March 2019): 12–22. http://dx.doi.org/10.1016/j.toxicon.2019.02.001.

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20

Roca, Amalia, Jose J. Rodríguez-Herva, and Juan L. Ramos. "Redundancy of Enzymes for Formaldehyde Detoxification in Pseudomonas putida." Journal of Bacteriology 191, no. 10 (March 20, 2009): 3367–74. http://dx.doi.org/10.1128/jb.00076-09.

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ABSTRACT Pseudomonas putida KT2440 exhibits redundant formaldehyde dehydrogenases and formate dehydrogenases that contribute to the detoxification of formaldehyde, a highly toxic compound. Physical and transcriptional analyses showed that the open reading frame (ORF) PP0328, encoding one of the formaldehyde dehydrogenases, is self-sufficient, whereas the other functional formaldehyde dehydrogenase gene (ORF PP3970) forms an operon with another gene of unknown function. Two formate dehydrogenase gene clusters (PP0489 to PP0492 and PP2183 to PP2186) were identified, and genes in these clusters were found to form operons. All four transcriptional promoters were mapped by primer extension and revealed the presence of noncanonical promoters expressed at basal level in the exponential growth phase and at a higher level in the stationary phase regardless of the presence of extracellular formaldehyde or formate. These promoters were characterized by a 5′-AG-CCA-C/A-CT-3′ conserved region between −7 and −16. To determine the contribution of the different gene products to formaldehyde and formate mineralization, mutants with single and double mutations of formaldehyde dehydrogenases were generated, and the effect of the mutations on formaldehyde catabolism was tested by measuring 14CO2 evolution from 14C-labeled formaldehyde. The results showed that both enzymes contributed to formaldehyde catabolism. A double mutant lacking these two enzymes still evolved CO2 from formaldehyde, suggesting the presence of one or more still-unidentified formaldehyde dehydrogenases. Mutants with single and double mutations in the clusters for formate dehydrogenases were also generated, and all of them were able to metabolize [14C]formate to 14CO2, suggesting a redundancy of functions that was not limited to only the annotated genes. Single and double mutants deficient in formaldehyde dehydrogenases and formate dehydrogenases exhibited longer lag phases than did the parental strain when confronted with concentrations of formaldehyde close to the MICs. This suggests a role for the detoxification system in tolerance to sublethal concentrations of formaldehyde.

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21

Petriello, Michael C., Jessie B. Hoffman, Andrew J. Morris, and Bernhard Hennig. "Emerging roles of xenobiotic detoxification enzymes in metabolic diseases." Reviews on Environmental Health 32, no. 1-2 (March 1, 2017): 105–10. http://dx.doi.org/10.1515/reveh-2016-0050.

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Abstract Mammalian systems have developed extensive molecular mechanisms to protect against the toxicity of many exogenous xenobiotic compounds. Interestingly, many detoxification enzymes, including cytochrome P450s and flavin-containing monooxygenases, and their associated transcriptional activators [e.g. the aryl hydrocarbon receptor (AhR)], have now been shown to have endogenous roles in normal physiology and the pathology of metabolic diseases. This mini-review will focus on two such instances: the role of flavin-containing monooxygenase 3 (FMO3) in the formation of the cardiometabolic disease biomarker trimethylamine-N-oxide (TMAO) and the role of AhR as a sensor of endogenous ligands such as those generated by the gut microbiota. Understanding the roles of xenobiotic sensing pathways in endogenous metabolism will undoubtedly lead to a better understanding of how exposure to environmental pollutants can perturb these physiological processes.

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22

Siegfried, Blair D., and Linda J. Young. "Activity of Detoxification Enzymes in Aquatic and Terrestrial Insects." Environmental Entomology 22, no. 5 (October 1, 1993): 958–64. http://dx.doi.org/10.1093/ee/22.5.958.

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23

Tomarev, S., R. Zinovieva, and J. Piatigorsky. "Recruitment of detoxification enzymes as lens crystallins in cephalopods." Experimental Eye Research 55 (September 1992): 151. http://dx.doi.org/10.1016/0014-4835(92)90730-g.

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24

Hart, Jonathan J., and Joseph M. Di Tomaso. "Sequestration and Oxygen Radical Detoxification as Mechanisms of Paraquat Resistance." Weed Science 42, no. 2 (June 1994): 277–84. http://dx.doi.org/10.1017/s0043174500080395.

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Evidence in the literature has generally supported either of two paraquat resistance mechanisms: an increase in activity of oxygen radical-scavenging enzymes in resistant plants which affords protection from active oxygen species formed by paraquat; and sequestration of paraquat away from its site of action in the chloroplast. Evidence for the first model relies primarily on measurement of increased enzyme activity and cross-resistance to other oxygen radical-generating stresses in resistant plants. The sequestration model is supported by data showing decreased translocation of paraquat and absence of paraquat injury in plant systems that do not have increased levels of protective enzymes. An alteration in paraquat transport at one of several plant cell membranes could confer resistance by modifying movement of paraquat into the compartment bounded by that membrane. Properties of the plasmalemma, chloroplast envelope, and tonoplast that may be important to paraquat transport are discussed and data supporting or discounting specific membrane alterations in resistant plants are presented. Finally, the possibility that both mechanisms may work in concert is addressed.

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25

Durak, Roma, Jan Dampc, Monika Kula-Maximenko, Mateusz Mołoń, and Tomasz Durak. "Changes in Antioxidative, Oxidoreductive and Detoxification Enzymes during Development of Aphids and Temperature Increase." Antioxidants 10, no. 8 (July 25, 2021): 1181. http://dx.doi.org/10.3390/antiox10081181.

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Temperature, being the main factor that has an influence on insects, causes changes in their development, reproduction, winter survival, life cycles, migration timing, and population dynamics. The effects of stress caused by a temperature increase on insects may depend on many factors, such as the frequency, amplitude, duration of the stress, sex, or the developmental stage of the insect. The aim of the study was to determine the differences in the enzymatic activity of nymphs and adult aphids Aphis pomi, Macrosiphum rosae and Cinara cupressi, and changes in their response to a temperature increase from 20 to 28 °C. The activity of enzymatic markers (superoxide dismutase (SOD), catalase (CAT), glutathione S-transferase (GST), β-glucosidase, polyphenol oxidase (PPO) and peroxidase (POD)) in aphid tissues was analysed for three constant temperatures. The results of our research showed that the enzymatic activity of aphids (measured as the activity of antioxidant, detoxifying and oxidoreductive enzymes) was mainly determined by the type of morph. We observed a strong positive correlation between the activity of the detoxifying and oxidoreductive enzymes and aphids’ development, and a negative correlation between the activity of the antioxidant enzymes and aphids’ development. Moreover, the study showed that an increase in temperature caused changes in enzyme activity (especially SOD, CAT and β-glucosidase), which was highest at 28 °C, in both nymphs and adults. Additionally, a strong positive correlation between metabolic activity (heat flow measured by microcalorimeter) and longevity was observed, which confirmed the relationship between these characteristics of aphids. The antioxidant enzyme system is more efficient in aphid nymphs, and during aphid development the activity of antioxidant enzymes decreases. The antioxidant enzyme system in aphids appears to deliver effective protection for nymphs and adults under stressful conditions, such as high temperatures.

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26

Liu, Siqi, Xiaolin Xu, Yanshun Kang, Yingtian Xiao, and Huan Liu. "Degradation and detoxification of azo dyes with recombinant ligninolytic enzymes from Aspergillus sp. with secretory overexpression in Pichia pastoris." Royal Society Open Science 7, no. 9 (September 2020): 200688. http://dx.doi.org/10.1098/rsos.200688.

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Ligninolytic enzymes, including laccase (Lac), manganese peroxidase (MnP) and lignin peroxidase (LiP), have attracted much attention in the degradation of contaminants. Genes of Lac (1827 bp), MnP (1134 bp) and LiP (1119 bp) were cloned from Aspergillus sp. TS-A, and the recombinant Lac (69 kDa), MnP (45 kDa) and LiP (35 kDa) were secretory expressed in Pichia pastoris GS115, with enzyme activities of 34, 135.12 and 103.13 U l −1 , respectively. Dyes of different structures were treated via the recombinant ligninolytic enzymes under the optimal degradation conditions, and the result showed that the decolourization rate of Lac on Congo red (CR) in 5 s was 45.5%. Fourier-transform infrared spectroscopy, gas chromatography–mass spectrometry analysis and toxicity tests further proved that the ligninolytic enzymes could destroy the dyes, both those with one or more azo bonds, and the degradation products were non-toxic. Moreover, the combined ligninolytic enzymes could degrade CR more completely compared with the individual enzyme. Remarkably, besides azo dyes, ligninolytic enzymes could also degrade triphenylmethane and anthracene dyes. This suggests that ligninolytic enzymes from Aspergillus sp. TS-A have the potential for application in the treatment of contaminants.

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27

Elaasser, M., and R. El Kassas. "Detoxification of aflatoxin B1 by certain bacterial species isolated from Egyptian soil." World Mycotoxin Journal 4, no. 2 (January 1, 2011): 169–76. http://dx.doi.org/10.3920/wmj2010.1262.

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Aflatoxin contamination of food and grain poses a serious economic and health problem worldwide. Aflatoxin B1 (AFB1) is extremely mutagenic, toxic and a potent carcinogen to both humans and livestock. A safe, effective and environmentally sound detoxification method is needed for controlling this toxin. In this study, 21 soil samples were screened from various sources with vast microbial populations using a coumarin containing medium. Eleven bacterial isolates showing AFB1 reduction activity in a liquid culture medium were selected from the screening experiments. Isolate 12-3 and 12-5, obtained from soil samples of Kafr-Zaiat Pesticide company drainage and identified to be Pseudomonas putida and Escherichia coli, reduced AFB1 by 69.3% and 58.8%, respectively, after incubation in the liquid medium at 37 °C for 72 h. The culture supernatant of these isolates was able to reduce AFB1 effectively by 76.2% and 62.5%, respectively, whereas the viable cells and cell extracts were far less effective. Factors influencing AFB1 detoxification by the culture supernatant were investigated. The highest detoxification activity for P. putida and E. coli was 83.3% and 63.8%, respectively, at pH 8 and 30 °C for 72 h. The detoxification activity was reduced at 10, 20 and 45 °C. The Mg2+, Mn2+, Se and Cu2+ ions were activators for AFB1 detoxification. However, Zn2+ ion was a strong inhibitor. Treatments with proteinase K, proteinase K plus SDS and heating significantly reduced or eradicated the detoxification activity of the culture supernatant. In conclusion, the detoxification of AFB1 by P. putida 12-3 was enzymatic and the enzymes responsible for the detoxification of AFB1 are constitutively extracellular produced. Also, the AFB1 detoxification by E. coli was conducted by enzymes as well as by cell wall binding mechanism. Both bacteria could have great potential in industrial applications.

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Li, Peng, Ruixue Su, Ruya Yin, Daowan Lai, Mingan Wang, Yang Liu, and Ligang Zhou. "Detoxification of Mycotoxins through Biotransformation." Toxins 12, no. 2 (February 14, 2020): 121. http://dx.doi.org/10.3390/toxins12020121.

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Mycotoxins are toxic fungal secondary metabolites that pose a major threat to the safety of food and feed. Mycotoxins are usually converted into less toxic or non-toxic metabolites through biotransformation that are often made by living organisms as well as the isolated enzymes. The conversions mainly include hydroxylation, oxidation, hydrogenation, de-epoxidation, methylation, glycosylation and glucuronidation, esterification, hydrolysis, sulfation, demethylation and deamination. Biotransformations of some notorious mycotoxins such as alfatoxins, alternariol, citrinin, fomannoxin, ochratoxins, patulin, trichothecenes and zearalenone analogues are reviewed in detail. The recent development and applications of mycotoxins detoxification through biotransformation are also discussed.

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29

Pedras, M. Soledade C., and Abbas Abdoli. "Pathogen inactivation of cruciferous phytoalexins: detoxification reactions, enzymes and inhibitors." RSC Advances 7, no. 38 (2017): 23633–46. http://dx.doi.org/10.1039/c7ra01574g.

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This review covers the detoxification pathways of cruciferous phytoalexins, the corresponding detoxifying enzymes and their natural and synthetic inhibitors. Paldoxins are examined as a potentially sustainable strategy to control plant pathogenic fungi.

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30

VanEtten, Hans D., Robert W. Sandrock, Catherine C. Wasmann, Scott D. Soby, Kevin McCluskey, and Ping Wang. "Detoxification of phytoanticipins and phytoalexins by phytopathogenic fungi." Canadian Journal of Botany 73, S1 (December 31, 1995): 518–25. http://dx.doi.org/10.1139/b95-291.

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Most plants synthesize antimicrobial compounds as part of normal plant development (i.e., phytoanticipins) or synthesize such compounds de novo when challenged by microorganisms (i.e., phytoalexins). The presumed role of these plant antibiotics is to protect the plant from disease. However, many phytopathogenic fungi have enzymes that can detoxify the phytoanticipins or phytoalexins produced by their host. This may be a means that these pathogens have evolved to circumvent resistance mechanisms based on the production of plant antibiotics. Many of the phytoanticipin- and phytoalexin-detoxifying enzymes produced by phytopathogenic fungi have biochemical and regulatory properties that would indicate the phytoanticipins and phytoalexins produced by their host are their normal substrates. In addition, their activity, enzymatic products, or transcripts can be detected in infected plant tissue suggesting that they are functioning in planta during pathogenesis. Specific mutations have been made by transformation-mediated gene-disruption procedures that eliminate the ability of Gaeumannomyces graminis var. avenae, Gloeocercospora sorghi, and Nectria haematococca to detoxify the phytoanticipins or phytoalexins produced by their hosts. The effect of these mutations on pathogenicity indicates a requirement for detoxifying enzymes in G. graminis var. avenae but not in G. sorghi or N. haematococca. Key words: disease resistance, pathogenicity mechanisms, isoflavonoids, saponins, cyanide.

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31

Bax, Bridget E. "Erythrocytes as Carriers of Therapeutic Enzymes." Pharmaceutics 12, no. 5 (May 8, 2020): 435. http://dx.doi.org/10.3390/pharmaceutics12050435.

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Therapeutic enzymes are administered for the treatment of a wide variety of diseases. They exert their effects through binding with a high affinity and specificity to disease-causing substrates to catalyze their conversion to a non-noxious product, to induce an advantageous physiological change. However, the metabolic and clinical efficacies of parenterally or intramuscularly administered therapeutic enzymes are very often limited by short circulatory half-lives and hypersensitive and immunogenic reactions. Over the past five decades, the erythrocyte carrier has been extensively studied as a strategy for overcoming these limitations and increasing therapeutic efficacy. This review examines the rationale for the different therapeutic strategies that have been applied to erythrocyte-mediated enzyme therapy. These strategies include their application as circulating bioreactors, targeting the monocyte–macrophage system, the coupling of enzymes to the surface of the erythrocyte and the engineering of CD34+ hematopoietic precursor cells for the expression of therapeutic enzymes. An overview of the diverse biomedical applications for which they have been investigated is also provided, including the detoxification of exogenous chemicals, thrombolytic therapy, enzyme replacement therapy for metabolic diseases and antitumor therapy.

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Noskov, Yu A., E. A. Chertkova, O. V. Polenogova, and O. N. Yaroslavtseva. "Синергетическое действие пиретроидного инсектицида и энтомопатогенного гриба на Daphnia magna Straus." Ukrainian Journal of Ecology 7, no. 4 (December 26, 2017): 393–98. http://dx.doi.org/10.15421/2017_133.

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<p>The interaction between the entomopathogenic fungus <em>Metarhizium robertsii</em> and the pyrethroid insecticide esfenvalerate on <em>Daphnia magna</em> Straus was investigated. A synergy in the mortality of daphnids was detected after simultaneous treatment with sub-lethal doses of the fungus (1×10<sup>5</sup> conidia/ml) and esfenvalerate (0.1 mkg/l). The defense strategies of daphnids infected by fungus and treated with esfenvalerate and untreated insects were compared to investigate the mechanisms of this synergy. Activity of enzymes of the detoxification system and concentration of dopamine were measured. We have shown changes in the activities of the enzymes and dopamine concentration of daphnids under combined treatment of esfenvalerate and fungus. Fungus enhanced activity of glutathione-S-transferase and non-specific esterase but did not affect the dopamine level. Esfenvalerate inhibited the activity of enzymes in the detoxification system and cause a rise in dopamine level. We assume that the suppression of the detoxification system may be one of the reasons of synergy between <em>M. robertsii</em> and esfenvalerate.</p>

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33

Misslinger, Matthias, Fabio Gsaller, Peter Hortschansky, Christoph Müller, Franz Bracher, Michael J. Bromley, and Hubertus Haas. "The cytochromeb5CybE is regulated by iron availability and is crucial for azole resistance inA. fumigatus." Metallomics 9, no. 11 (2017): 1655–65. http://dx.doi.org/10.1039/c7mt00110j.

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Smirle, Michael J., and Mark L. Winston. "Detoxifying enzyme activity in worker honey bees: an adaptation for foraging in contaminated ecosystems." Canadian Journal of Zoology 66, no. 9 (September 1, 1988): 1938–42. http://dx.doi.org/10.1139/z88-283.

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The activities of two important groups of detoxifying enzymes, the glutathione S-transferases and the mixed-function oxidases, were assayed throughout the lifetimes of worker honey bees (Apis mellifera L.). Detoxification capacity decreased on a per insect basis in older workers and was associated with a dramatic loss of midgut protein. However, analysis of specific activity (enzyme activity per milligram protein) showed increasing activity levels as bees aged and began to forage. These results show that foraging worker honey bees compensate for protein loss by increasing the activity of important enzymes, suggesting a possible biochemical adaptation for foraging in contaminated ecosystems.

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35

Altay, Ahmet, Kartal İrtem, Gökhan Sadi, Tülin Güray, and Ahmet Yaprak. "Modulation of mRNA expression and activities of xenobiotic metabolizing enzymes, CYP1A1, CYP1A2, CYP2E1, GPx and GSTP1 by the Salicornia freitagii extract in HT-29 human colon cancer cells." Archives of Biological Sciences 69, no. 3 (2017): 439–48. http://dx.doi.org/10.2298/abs160825118a.

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Phase I-II detoxification and antioxidant enzymes are responsible for the detoxification and elimination of activated carcinogens, acting as important biomarkers for chemoprevention. Among them, cytochrome P450s plays a prominent role in the metabolic activation of xenobiotics. The herb Salicornia freitagii (SF) (Amaranthaceae) is known for its anticancer, antioxidant, antidiabetic and antiinflammatory activities. In this study, we determined the bioactive phenolics in the SF methanol extract and investigated its antiproliferative potential in HT-29 human colon cancer cells. We also investigated the modulation of some phase I and II enzyme (CYP 1A1, 1A2, 2E1, GSTP1 and GPx) mRNA expression and enzymatic activities by the SF extract and its major bioactive phenolic compounds. LC/MS-MS analysis showed that the main phenolic compounds of the methanolic SF extract are vanillic acid (48 ?g/100g) and p-coumaric acid (10.8 ?g/100g). SF extract, vanillic acid and p-coumaric acid exhibited high antiproliferative activities in HT-29 cells, with IC50 values of 81.79?g/mL, 98.8 ?M and 221.6 ?M, respectively. The mRNA expression levels of CYP1A2 and CYP2E1 were decreased, while those of GSTP1 and GPx in HT-29 cells were increased after application of either the SF extract or vanillic acid. The SF extract by itself also increased the activities of GPx and GSTP1 enzymes 1.68- and 1.49-fold, respectively. Our data indicate that the SF extract and its major bioactive compound, vanillic acid, could exert a modulatory effect on the expression of enzymes that are involved in xenobiotic activation and detoxification pathways in the gastrointestinal tract. For this reason, SF can be considered as a natural source of chemopreventive agents.

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Usui, Kenji. "Metabolic herbicide resistance and related detoxification enzymes in grass weeds." Journal of Weed Science and Technology 63, no. 1 (2018): 1–2. http://dx.doi.org/10.3719/weed.63.1.

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Gorbi, Stefania, David Pellegrini, Sara Tedesco, and Francesco Regoli. "Antioxidant efficiency and detoxification enzymes in spotted dogfish Scyliorhinus canicula." Marine Environmental Research 58, no. 2-5 (August 2004): 293–97. http://dx.doi.org/10.1016/j.marenvres.2004.03.074.

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Wackett, Lawrence P. "Recruitment of Co-Metabolic Enzymes for Environmental Detoxification of Organohalides." Environmental Health Perspectives 103 (June 1995): 45. http://dx.doi.org/10.2307/3432478.

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Liu, Da-Ling, Dong-Sheng Yao, Ren Liang, Lin Ma, Wei-Qiang Cheng, and Lian-Quan Gu. "Detoxification of Aflatoxin B1 by Enzymes Isolated from Armillariella tabescens." Food and Chemical Toxicology 36, no. 7 (July 1998): 563–74. http://dx.doi.org/10.1016/s0278-6915(98)00017-9.

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Wackett, L. P. "Recruitment of co-metabolic enzymes for environmental detoxification of organohalides." Environmental Health Perspectives 103, suppl 5 (June 1995): 45–48. http://dx.doi.org/10.1289/ehp.95103s445.

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41

Kreuz, K., R. Tommasini, and E. Martinoia. "Old Enzymes for a New Job (Herbicide Detoxification in Plants)." Plant Physiology 111, no. 2 (June 1, 1996): 349–53. http://dx.doi.org/10.1104/pp.111.2.349.

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Fabiani, Emiliano, Francesco D’Alò, Alessandra Scardocci, Mariangela Greco, Annalisa Di Ruscio, Marianna Criscuolo, Luana Fianchi, et al. "Polymorphisms of detoxification and DNA repair enzymes in myelodyplastic syndromes." Leukemia Research 33, no. 8 (August 2009): 1068–71. http://dx.doi.org/10.1016/j.leukres.2008.10.012.

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43

Jin, Yongling, Yugang Gao, Haiyan Zhang, Liyan Wang, Kejun Yang, and Hui Dong. "Detoxification enzymes associated with butene‐fipronil resistance in Epacromius coerulipes." Pest Management Science 76, no. 1 (August 14, 2019): 227–35. http://dx.doi.org/10.1002/ps.5500.

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44

Kawamoto, Yoshiyuki, Yoshimasa Nakamura, Yuko Naito, Yasuyoshi Torii, Takeshi Kumagai, Toshihiko Osawa, Hajime Ohigashi, Kimihiko Satoh, Masayoshi Imagawa, and Koji Uchida. "Cyclopentenone Prostaglandins as Potential Inducers of Phase II Detoxification Enzymes." Journal of Biological Chemistry 275, no. 15 (April 6, 2000): 11291–99. http://dx.doi.org/10.1074/jbc.275.15.11291.

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45

Dec, J., and J. M. Bollag. "Detoxification of substituted phenols by oxidoreductive enzymes through polymerization reactions." Archives of Environmental Contamination and Toxicology 19, no. 4 (1990): 543–50. http://dx.doi.org/10.1007/bf01059073.

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46

Niranjan, Vidya, Akshay Uttarkar, Sujitha Dadi, Akashata Dawane, Ashwin Vargheese, Jalendra Kumar H. G., Udayakumar Makarla, and Vemanna S. Ramu. "Stress-Induced Detoxification Enzymes in Rice Have Broad Substrate Affinity." ACS Omega 6, no. 4 (January 20, 2021): 3399–410. http://dx.doi.org/10.1021/acsomega.0c05961.

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Wang, Xianzhe, Xumei Wang, Yanyan Zhu, and Xiuping Chen. "ADME/T-based strategies for paraquat detoxification: Transporters and enzymes." Environmental Pollution 291 (December 2021): 118137. http://dx.doi.org/10.1016/j.envpol.2021.118137.

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48

Hasan, Khomaini. "A mini review of haloalkane dehalogenase: From molecular characterization to applications." Communications in Science and Technology 3, no. 1 (June 14, 2018): 15–18. http://dx.doi.org/10.21924/cst.3.1.2018.70.

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Haloalkane dehalogenases (HLDs) are hydrolytic enzymes that catalyze a removal of halogenated species in many toxic halogenated compounds. These enzymes belong to hydrolase family that mostly adopt a typically a/b hydrolase structure. They have many potential applications, such as industrial biocatalysis, pharmaceutics, biosensors, or detoxification of chemical weapons. In this review, structure, mechanism and applications of these enzymes will be discussed.

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Gao, Liu, Jiang, Fu, Zhao, Li, and Ye. "Protective Responses Induced by Chiral 3-Dichloroacetyl Oxazolidine Safeners in Maize (Zea mays L.) and the Detoxification Mechanism." Molecules 24, no. 17 (August 22, 2019): 3060. http://dx.doi.org/10.3390/molecules24173060.

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Herbicide safeners selectively protect crops from herbicide injury while maintaining the herbicidal effect on the target weed. To some extent, the detoxification of herbicides is related to the effect of herbicide safeners on the level and activity of herbicide target enzymes. In this work, the expression of the detoxifying enzyme glutathione S-transferase (GST) and antioxidant enzyme activities in maize seedlings were studied in the presence of three potential herbicide safeners: 3-dichloroacetyl oxazolidine and its two optical isomers. Further, the protective effect of chiral herbicide safeners on detoxifying chlorsulfuron in maize was evaluated. All safeners increased the expression levels of herbicide detoxifying enzymes, including GST, catalase (CAT), and peroxidase (POD) to reduce sulfonylurea herbicide phytotoxicity in maize seedlings. Our results indicate that the R-isomer of 3-(dichloroacetyl)-2,2,5-trimethyl-1,3-oxazolidine can induce glutathione (GSH) production, GST activity, and the ability of GST to react with the substrate 1-chloro-2,4-dinitrobenzene (CDNB) in maize, meaning that the R-isomer can protect maize from damage by chlorsulfuron. Information about antioxidative enzyme activity was obtained to determine the role of chiral safeners in overcoming the oxidative stress in maize attributed to herbicides. The interaction of safeners and active target sites of acetolactate synthase (ALS) was demonstrated by molecular docking modeling, which indicated that both isomers could form a good interaction with ALS. Our findings suggest that the detoxification mechanism of chiral safeners might involve the induction of the activity of herbicide detoxifying enzymes as well as the completion of the target active site between the safener and chlorsulfuron.

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Hinson, Jack A., and Poh-Gek Forkert. "Phase II enzymes and bioactivation." Canadian Journal of Physiology and Pharmacology 73, no. 10 (October 1, 1995): 1407–13. http://dx.doi.org/10.1139/y95-196.

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A colloquium entitled Phase II enzymes and bioactivation was held during the 10th International Symposium on Microsomes and Drug Oxidations in Toronto, Ont., on July 20, 1994. This colloquium was a tribute in recognition of the contributions by Dr. James R. Gillette in advancing our understanding of drug metabolism and chemical toxicity. A major focus of the colloquium was formation of conjugates such as those with glutathione (GSH) that may not lead to detoxification but to bioactivation. The GSH conjugates may be further metabolized to reactive species that cause toxicity. The nephrotoxicity of hydroquinone and bromobenzene is mediated via quinine–glutathione conjugates, and is manifested in cellular changes, including induction of the gadd-153 and hsp-70 mRNA. The formation of GSH conjugates is also involved in the bioactivation of the vicinal dihalopropane 1,2-dibromo-3-chloropropane; cytotoxic lesions are observed in the kidney and testes. The evidence indicates that conjugation is mediated by the GSH S-transferases. The symposium also covered aspects of the importance of conjugation in the pharmacokinetics of certain drugs. Conjugation reactions including sulfation are markedly influenced by the manner in which the liver processes the drug. Characteristics such as erythrocyte binding, as in the case of acetaminophen, become limiting factors in the conjugation reactions. Conjugation reactions can lead to a different outcome, such as acquired drug resistance. Conjugation of metallothioneins with the alkylating mustard drugs melphalan and chlorambucil can lead to the formation of protein adducts. Conjugation of reactive intermediates with these small molecular weight proteins may be considered as a phase II reaction and a mechanism of detoxification. A different pathway for the metabolism of xenobiotics is catalyzed by the carboxylesterases, a family of enzymes that is involved in hydrolysis of chemical compounds, generally leading to detoxification. Three rat esterases have been purified, cloned, and characterized. Two forms, hydrolase A and hydrolase B, are present in liver microsomes in a number of species, including the human. These are also detected in extrahepatic tissues. A third esterase, hydrolase S, is found in rat liver microsomes and rat serum, and may be a serum carboxylesterase secreted from the liver. A better knowledge of esterases will advance our understanding of pharmacokinetics and mechanisms of the effects of chemicals such as phenacetin and acetaminophen, two drugs that Dr. Gillette has worked with extensively. The data presented herein reflect the new and innovative approaches that have been adopted to investigate various aspects of chemical toxicity and drug metabolism. These data also indicate that significant insights are likely to come from integrated approaches utilizing established toxicological techniques together with those from other disciplines, including molecular biology and analytical chemistry.Key words: drug metabolism, drug disposition, toxicity, conjugation.

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