Esterase

(redirected from Esterases)
Also found in: Dictionary, Medical.

esterase

[′es·tə‚rās]
(biochemistry)
Any of a group of enzymes that catalyze the synthesis and hydrolysis of esters.

Esterase

 

any of the enzymes of the hydrolase class that catalyze the cleavage of the ester bond in organic compounds. In the broad sense of the word, esterases include lipases, phosphatases, and sulfatases, in addition to esterases proper, among which are many specific enzymes, such as cholinesterase, chlorophyllase, tannase, and pectinase. Esterases are found in humans, animals, higher plants, and microorganisms. In humans and animals, they are found in pancreatic juice (pancreatic lipase, or steapsin), blood, and milk; they are also found in the liver, the intestinal walls, and various tissues.

References in periodicals archive ?
We found statistically significant correlations between increased resistance to 5-fluorocytosine and higher enzymatic activity of alkaline phosphatase, chymotrypsin, and alpha-glucosidase; increased resistance to fluconazole and higher enzymatic activity of esterase and beta-glucosidase as well as increased susceptibility to ketoconazole and higher enzymatic activity of cystine arylamidase; increased susceptibility to fluconazole and higher enzymatic activity of mannosidase.
The increased level of esterases in phosphine tolerant populations as compared to susceptible population has pointed some correlation between esterase activities and phosphine tolerance.
The urine strip test reaction for leucocytes is based on the action of leucocyte esterase in catalysing the hydrolysis of an ester of indolecarboxylic acid.
Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families.
Bacillus subtilis KPA-1 was used in present study for esterase production which was isolated from farm soil samples by enrichment culture technique.
Specific inhibitor tests for the biochemical and functional classification of esterases by PAGE have distinguished carboxylesterases (Est-2, Est-3, Est-5, Est-6, Est-7, Est-8, Est-9, Est-10, and Est-16 isozymes) and acetylesterases (Est-4, Est-11, Est-12, Est-13, Est14, Est-15 isozymes) in grapes (ORASMO et al.
We measured the response of 3 detoxifying enzyme systems: general esterase (EST), glutathione S-transferase (GST), and cytochrome P450 monooxygenase (P450).
The activity of esterases in the gut was reduced in chlorpyrifos exposed termite worker, whereas proteases and cellulases in these workers remained non- significant with their control treatments.
In order to obtain indirect information about the existence and intensity of genetic exchange between different regions and about the presence of insecticide resistance, the purpose of the current research is to determine the variability in esterase activity in greenbug populations collected from very contrasting regions of Argentina and Chile in autumn and spring since 1987.
Furthermore, because Calcein-AM test results could be influenced by changes in esterase activity, DC extracts, as well pure harpagoside were tested for a possible inhibition of this enzyme.
Esterases are enzymes which catalyse the hydrolytic breakdown of ester bonds.