A p -coumaroyl esterase from Rhizoctonia solani with a pronounced chlorogenic acid esterase activity

2017 ◽  
Vol 37 ◽  
pp. 153-161 ◽  
Author(s):  
Annabel Nieter ◽  
Sebastian Kelle ◽  
Diana Linke ◽  
Ralf G. Berger
Keyword(s):  
Rhizoctonia Solani ◽  
Chlorogenic Acid ◽  
Esterase Activity

scholarly journals Cutinase and Other Lipolytic Esterases Protect Bean Leaves from Infection by Rhizoctonia solani

1998 ◽  
Vol 11 (6) ◽  
pp. 514-522 ◽  
Author(s):  
Diana M. Parker ◽  
Wolfram Köller
Keyword(s):  
Rhizoctonia Solani ◽  
Esterase Activity ◽  
Venturia Inaequalis ◽  
Protective Mechanism ◽  
Disease Development ◽  
Mechanical Wounding ◽  
Small Areas ◽  
Pathogenesis Related ◽  
Web Blight ◽  
Bean Leaves

The results describe a novel activity of fungal cutinase, the protection of bean leaves from disease. Development of web blight symptoms on bean leaves infected with Rhizoctonia solani (AG-1) was prevented in the presence of cutinase purified from Venturia inaequalis. Instead of disease, small areas of tissue necrosis became visible, and the tissue in which the pathogen was restricted displayed strong autofluorescence beneath the inoculation sites. Mechanical wounding of the leaf surface had no effect on disease development and the permeability of the cuticle was not increased by cutinase action, indicating that surface wounding was not the cause for this novel activity of cutinase. A comparative study involving cutinase and other serine hydrolases revealed that the disease prevention resided in the lipolytic esterase activity rather than the cutinase activity. The pattern of expression of four pathogenesis-related (PR) protein genes provided no evidence for the modulation of known resistance responses of bean leaves in response to cutinase action. The protective mechanism of the esterase activity remains unknown.

scholarly journals Hydrolysis of chlorogenic acid in apple juice using a p ‐coumaryl esterase of Rhizoctonia solani

2019 ◽  
Vol 99 (14) ◽  
pp. 6644-6648
Author(s):  
Mareike Siebert ◽  
Ralf Günter Berger ◽  
Franziska Pfeiffer
Keyword(s):  
Rhizoctonia Solani ◽  
Chlorogenic Acid ◽  
Apple Juice ◽  
Hydrolysis Of

Silicon Mediated Resistance to Rice Sheath Blight by Increasing Ferulic Acid and Chlorogenic Acid

2012 ◽  
Vol 550-553 ◽  
pp. 1274-1277
Author(s):  
Guo Liang Zhang
Keyword(s):  
Disease Resistance ◽  
Ferulic Acid ◽  
Rhizoctonia Solani ◽  
Chlorogenic Acid ◽  
Sheath Blight ◽  
Disease Index ◽  
Susceptible Cultivar ◽  
Rice Sheath Blight ◽  
As If

Silicon (Si) can enhance the resistance to rice sheath blight causing by Rhizoctonia solani (R. solani), but ferulic acid and chlorogenic acid involved in disease resistance with Si application on is scarcely known. The susceptible cultivar Ningjing 1 was selected to determine the effects of Si on disease index of rice sheath blight as well as if ferulic acid and chlorogenic acid were involved in disease resistance. The results showed that Si application reduced the disease index of sheath blight by 15.62. For uninoculated plants, Si application alone did not change the concentration of ferulic acid and chlorogenic acid significantly. For inoculated plants, Si application increased the concentration of ferulic acid and chlorogenic acid significantly. It is conclued that the important way of Si mediated resistance in rice against sheath blight is probably through increasing ferulic acid and chlorogenic acid.

Tobacco Mosaic Virus-Infected Tissue

1985 ◽  
Vol 43 ◽  
pp. 510-511
Author(s):  
Egbert W. Henry
Keyword(s):  
Nicotiana Tabacum ◽  
Tobacco Mosaic Virus ◽  
Chlorogenic Acid ◽  
Mosaic Virus ◽  
Host Resistance ◽  
Oxidative Metabolism ◽  
Leaf Tissue ◽  
Vein Clearing ◽  
Basal Septum ◽  
Concentration Levels

Tobacco mosaic virus (TMV) infection has been studied in several investigations of Nicotiana tabacum leaf tissue. Earlier studies have suggested that TMV infection does not have precise infective selectivity vs. specific types of tissues. Also, such tissue conditions as vein banding, vein clearing, liquification and suberization may result from causes other than direct TMV infection. At the present time, it is thought that the plasmodesmata, ectodesmata and perhaps the plasmodesmata of the basal septum may represent the actual or more precise sites of TMV infection.TMV infection has been implicated in elevated levels of oxidative metabolism; also, TMV infection may have a major role in host resistance vs. concentration levels of phenolic-type enzymes. Therefore, enzymes such as polyphenol oxidase, peroxidase and phenylalamine ammonia-lyase may show an increase in activity in response to TMV infection. It has been reported that TMV infection may cause a decrease in o-dihydric phenols (chlorogenic acid) in some tissues.

Study of Thrombin-Coagulase

1967 ◽  
Vol 17 (03/04) ◽  
pp. 321-334 ◽  
Author(s):  
J. P Soulier ◽  
Odette Prou-Wartelle ◽  
Liliane Hallé ◽  
Keyword(s):  
Esterase Activity ◽  
Adsorption Chromatography ◽  
The Difference

SummaryThe preparation of thrombin-coagulase is described. The properties of thrombin-coagulase are compared with those of biothrombin: kinetics, thermostability, adsorption, chromatography, esterase activity, clotting activity, action on platelets and on factors V and VIII, susceptibility to inhibitors.Biothrombin and thrombin-coagulase are closely related but distinct. Both apparently derive from prothrombin. Prothrombin and coagulase combine to form a complex: thrombin-coagulase wherein both factors are necessary for its activity. Possible explanations for the difference between thrombin-coagulase and biothrombin are proposed.

Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine Esters

1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher
Keyword(s):  
Molecular Structure ◽  
Methyl Ester ◽  
Comparative Studies ◽  
Esterase Activity ◽  
Methyl Esters ◽  
Hydrolytic Activity ◽  
The Other ◽  
Other Hand

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.

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