Functional analysis of H2O2-generating systems in Botrytis cinerea: the major Cu-Zn-superoxide dismutase (BCSOD1) contributes to virulence on French bean, whereas a glucose oxidase (BCGOD1) is dispensable

The aim of this study was to evaluate the bioremoval of anthracycline antibiotics (daunomycin-DNR, doxorubicin–DOX, and mitoxantrone-MTX) by immobilized mycelium of B. adusta CCBAS 930. The activity of oxidoreductases: versatile peroxidases (VP), superoxide dismutase (SOD), catalase (CAT), and glucose oxidase (GOX), and the levels of phenolic compounds (PhC) and free radicals (SOR) were determined during the biotransformation of anthracyclines by B. adusta strain CCBAS 930. Moreover, the phytotoxicity (Lepidium sativum L.), biotoxicity (MARA assay), and genotoxicity of anthracyclines were evaluated after biological treatment. After 120 h, more than 90% of anthracyclines were removed by the immobilized mycelium of B. adusta CCBAS 930. The effective biotransformation of anthracyclines was correlated with detoxification and reduced genotoxicity.

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Comparison of defence responses to Botrytis cinerea infection in tomato plants propagated in vitro and grown in vivo

Acta Agrobotanica ◽

10.5586/aa.1996.012 ◽

2013 ◽

Vol 49 (1-2) ◽

pp. 115-121 ◽

Cited By ~ 1

Author(s):

Jacek Patykowski ◽

Elżbieta Kuźniak ◽

Henryk Urbaniak

Keyword(s):

Superoxide Dismutase ◽

Botrytis Cinerea ◽

Ascorbate Peroxidase ◽

Guaiacol Peroxidase ◽

Activity Increase ◽

Tomato Plants ◽

Defence Responses ◽

Defence Reactions

Defence reactions: O2 - generation, superoxide dismutase, catalase, guaiacol peroxidase and ascorbate peroxidase activities after B. cinerea infection in tomato plants propagated in vitro and grown in vivo have been compared. Infection resulted in rapid O2 - generation. Superoxide dismutase activity increase was slower than O2 - response. In plants propagated in vitro catalase and guaiacol peroxidase activities after infection were induced less strongly than in plants grown in vivo. K2HPO4 pretreatment of plants grown in vitro enhanced significantly the activities of catalase and guaiacol peroxidase after infection. Slight restriction of B. cinerea infection development in in vitro propagated plants pretreated with K2HP04 was observed.

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Functional analysis of the β 2 -tubulin gene of Fusarium graminearum and the β -tubulin gene of Botrytis cinerea by homologous replacement

Pest Management Science ◽

10.1002/ps.3474 ◽

2013 ◽

Vol 69 (5) ◽

pp. 582-588 ◽

Cited By ~ 38

Author(s):

ShengMing Liu ◽

YaBing Duan ◽

ChangYan Ge ◽

ChangJun Chen ◽

MingGuo Zhou

Keyword(s):

Functional Analysis ◽

Botrytis Cinerea ◽

Fusarium Graminearum ◽

Tubulin Gene ◽

Β Tubulin

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Glucose oxidase as a control agent against the fungal pathogen Botrytis cinerea in postharvest strawberry

Food Control ◽

10.1016/j.foodcont.2019.05.037 ◽

2019 ◽

Vol 105 ◽

pp. 277-284 ◽

Cited By ~ 6

Author(s):

Xiaojing Li ◽

Xinfang Xie ◽

Fuguo Xing ◽

Ling Xu ◽

Jie Zhang ◽

...

Keyword(s):

Glucose Oxidase ◽

Botrytis Cinerea ◽

Fungal Pathogen ◽

Control Agent

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Hemolysis and iodination of erythrocyte components by a myeloperoxidase- mediated system

Blood ◽

10.1182/blood.v45.5.699.699 ◽

1975 ◽

Vol 45 (5) ◽

pp. 699-707 ◽

Cited By ~ 41

Author(s):

SJ Klebanoff ◽

RA Clark

Keyword(s):

Superoxide Dismutase ◽

Thyroid Hormones ◽

Glucose Oxidase ◽

Xanthine Oxidase ◽

Combined Effect ◽

Oxidase System ◽

Generating System

Abstract Erythrocytes are hemolyzed by myeloperoxidase, an H2O2-generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). The combined effect of chloride and either iodide or the thyroid hormones is greater than additive. Myeloperoxidase can be replaced by lactoperoxidase in the iodide-, thyroxine and triiodothyronine- dependent, but not in the chloride-dependent, systems. Hemolysis is is inhibited by the peroxidase inhibitors, azide and cyanide, and by catalase and is stimulated by superoxide dismutase when the xanthine oxidase system is employed as the source of H2O2. Hemolysis by the iodide-dependent system is associated with the iodination of erythrocyte components.

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