Lipolytic enzymes, esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3), catalyze the hydrolysis of ester bonds between alcohols and carboxylic acids, and its formation in organic media. At present, they represent about 20% of commercialized enzymes for industrial use. Lipolytic enzymes from thermophilic microorganisms are preferred for industrial use to their mesophilic counterparts, mainly due to ...

Proteins and various isozymes were investigated by direct analysis of single specimens in order to check molecular genetic variability, which is not rare in Meloidogyne species in spite of parthenogenetic reproduction. Variability was found in esterases, ocglycerophosphate, malate dehydrogenases, and some other proteins. Other loci appear monomorphic in the genus (for example, catalase), Distin...

A sample of Aedes aegypti (L.) from Santiago de Cuba, Cuba, with a high level of temephos resistance (19.58x at the 50% lethal concentration [LC50]), was subjected to temephos selection to evaluate the utility of this organophosphate insecticide for mosquito control. High resistance developed after six generations of selection (200.00x). Little or no cross-resistance was observed to the organop...

The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 degrees C respectively. Divalent cations were not required for the enzyme activity....

Twelve populations of Heterodera glycines from the United States (8), China (2), Japan (1), and Colombia (1) were surveyed for phenotypic intraspecific variability in 42 enzyme systems. Activity of 20 enzymes was detected following isoelectric focusing in polyacrylamide gels of extracts from mass homogenates and single females. Five enzymes, aspartate aminotransferase, phosphoglucose isomerase,...