Purification and Characterization of a Novel Extracellular Lipase Catalyzing Hydrolysis of Oleyl Benzoate fromAcinetobacternov. sp. Strain KM109

A Novel Alkaline Esterase fromSporosarcinasp. nov. Strain eSP04 Catalyzing the Hydrolysis of a Wide Variety of Aryl-carboxylic Acid Esters

“…The substrate specificities of a large number of carboxylesterases have been documented. 3,5) Reports on aryl-carboxylesterases showing activities for the esters of aryl-carboxylic acids containing an aromatic ring next to the ester carboxyl group, such as ethyl benzoate (EBz), are very limited [7][8][9][10][11] compared with those on ordinary aliphatic carboxylesterases. The enzymes hydrolyzing phthalic acid esters, which are potential environmental pollutants, may be one exceptional aryl-carboxylesterase studied in many research groups.…”

“…The enzymes hydrolyzing phthalic acid esters, which are potential environmental pollutants, may be one exceptional aryl-carboxylesterase studied in many research groups. [12][13][14][15][16] In addition, the aryl-carboxylesterases thus far reported appeared to have rather narrow substrate specificity, or the substrates studied with the enzymes are limited in structure, [7][8][9][10][11] when one considers the occurrence of a large number of structurally analogous arylcarboxylic acid esters. Enzymes hydrolyzing 4-hydroxybenzoic acid esters are considered to belong to a different esterase family from benzoyl esterases.…”

An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity

“…There is no consistent nomenclature for benzoyl esterases. They are reported as enzymes hydrolyzing benzoyl esters of simple sugars [12], as lipases acting on oleyl benzoate [13] and esterases cleaving 4-hydroxybenzoic acid esters [14]. Applications of benzoyl esterases are the enantioselective synthesis of flavors, fine chemicals and pharmaceuticals [4,15].…”

Converting human carbonic anhydrase II into a benzoate ester hydrolase through rational redesign

“…By using an enzyme that hydrolyzes a benzoate ester bond in the cocaine molecule, the level of biologically active drug substance can be lowered rapidly. [4] Notably, several commonly used lipases lack any appreciable activity with model benzoate ester substrates, such as paranitrophenyl benzoate, [5] and many groups perform work on the identification and development of lipase variants with activity against bulky substrates. [5][6][7] In this report, we expand the range of enzymes able to hydrolyze benzoate esters by adding a human carbonic anhydrase II (HCAII) variant.…”

“…[4] Notably, several commonly used lipases lack any appreciable activity with model benzoate ester substrates, such as paranitrophenyl benzoate, [5] and many groups perform work on the identification and development of lipase variants with activity against bulky substrates. [5][6][7] In this report, we expand the range of enzymes able to hydrolyze benzoate esters by adding a human carbonic anhydrase II (HCAII) variant. The physiological role of the zinc enzyme HCAII (CA; carbonate hydro-lyase, EC 4.2.1.1) is to catalyze the reversible hydration of carbon dioxide: CO 2 + H 2 O ↔ HCO 3 -+ H + .…”