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Utilisation of mango seed husk for the production of phenolic compounds and glucose with C1184 enzyme preparation reveals the role of glucuronoyl esters in lignin-carbohydrate linkages in biomass recalcitrance. [PDF]
Bioresour BioprocessMafa MS +4 more
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Larval habitat drives differential selection pressures on genetic insecticide resistance and metabolic enzyme plasticity in Anopheles gambiae s.l during laboratory colonization. [PDF]
Sci RepGyimah IK +15 more
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Biochemical Genetics, 1982
The comparison of results obtained by different separation and staining techniques permits the definition of esterase-6 in comparison with esterase-9 and a new esterase, esterase-20. Alleles of Es-6 affect the product's ability to aggregate. Esterase-20 may be an aggregated product of Es-9. The close linkage of Es-6 and Es-9 is confirmed.
O von Deimling
exaly +3 more sources
The comparison of results obtained by different separation and staining techniques permits the definition of esterase-6 in comparison with esterase-9 and a new esterase, esterase-20. Alleles of Es-6 affect the product's ability to aggregate. Esterase-20 may be an aggregated product of Es-9. The close linkage of Es-6 and Es-9 is confirmed.
O von Deimling
exaly +3 more sources
Esterases as stereoselective biocatalysts
Biotechnology Advances, 2015 Non-lypolitic esterases are carboxylester hydrolases with preference for the hydrolysis of water-soluble esters bearing short-chain acyl residues. The potential of esterases as enantioselective biocatalysts has enlarged in the last few years due to the ...
Thiago de Sousa Fonseca +2 more
exaly +2 more sources
CRC Critical Reviews in Clinical Laboratory Sciences, 1979
Esterases are enzymes that cleave aliphatic and aromatic ester bonds. With the use of synthetic substrates, esterases can be demonstrated in hematopoietic cells. Using alpha naphthyl acetate or alpha naphthyl butyrate, nonspecific esterase activity can be demonstrated.
Lawrence Kass, John G. Batsakis
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Esterases are enzymes that cleave aliphatic and aromatic ester bonds. With the use of synthetic substrates, esterases can be demonstrated in hematopoietic cells. Using alpha naphthyl acetate or alpha naphthyl butyrate, nonspecific esterase activity can be demonstrated.
Lawrence Kass, John G. Batsakis
openaire +2 more sources
Canadian Journal of Biochemistry, 1969
Esterases produced by eight species of fungi are capable of hydrolyzing the benzoyl esters of simple sugars. These benzoyl esterases are of two types based on their specificities. One type acts on a broad band of benzoyl esters, including benzoylcholine, and is found only in Aspergillus terricola.
E T, Reese, A, Maguire, F W, Parrish
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Esterases produced by eight species of fungi are capable of hydrolyzing the benzoyl esters of simple sugars. These benzoyl esterases are of two types based on their specificities. One type acts on a broad band of benzoyl esters, including benzoylcholine, and is found only in Aspergillus terricola.
E T, Reese, A, Maguire, F W, Parrish
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Esterases in fireflies and their inhibition
Archives of Biochemistry and Biophysics, 1961Abstract Homogenized tissues of fireflies contain an aliesterase and a cholinesierase. The first enzyme is distributed throughout the body; the second one is concentrated mainly in the head. The aliesterase was inhibited by DFP and by the carbamate-type insecticides, Isolan and Sevin.
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