Abstract A novel esterase which is derived from Serratia marcescens is disclosed. Said esterase has the following physico-chemical properties and enzymatic characteristics: (1) Activity; it (i.e., said esterase) hydrolyzes an ester bond of organic carboxylates, (2) Substrate specificity; it acts on alkyl esters of organic carboxylic acids, triglycerides or thiol esters, (3) Optimum pH; its optimum pH is 7.5-9.0 when the hydrolysis is carried out by using olive oil as the substrate, (4) pH stability; it is stable at pH 5.0-9.0 when it is stored at 30° C. for one hour, (5) Optimum temperature; its optimum temperature is 40°-50° C. when the hydrolysis is carried out by using olive oil as the substrate, (6) Heat stability; it is stable at a temperature of not higher than 50° C. when it is stored at pH 8.0 for 30 minutes, (7) Molecular weight; 62,000±2,000 (SDS-polyacrylamide gel electrophoresis), (8) Isoelectric point; 4.6±0.1, (9) Effect of metal ions; it is activated in the presence of 1 mM calcium ion, and inhibited in the presence of 1 mM cobalt ion, nickel ion, iron ion or ethylenediamine-tetraacetic acid. Said esterase can widely be applied for organic synthetic reactions.
An essentially purified esterase derived from Serratia marcescens Sr41 (FERM BP-No. 487) having the following physico-chemical properties and enzymatic characteristics: (1) Activity: said esterase hydrolyzes an ester bond of organic carboxylates, (2) Substrate specificity: said esterase acts on alkyl esters of organic carboxylic acids, triglycerides or thiol esters, (3) Optimum pH: said esterase has an optimum pH of 7.5-9.0 when the hydrolysis is carried out using olive oil as the substrate, (4) pH stability: said esterase is stable at pH 5.0-9.0 when it is stored at 30° C. for one hour, (5) Optimum temperature: said esterase has an optimum temperature of 40°-50° C. when the hydrolysis is carried out using olive oil as the substrate, (6) Heat stability: said esterase is stable at a temperature of not higher than 50° C. when it is stored at pH 8.0 for 30 minutes, (7) Molecular weight: 62,000±2,000 (SDS-polyacrylamide gel electrophoresis), (8) Isoelectric point: 4.6±0.1, (9) Effect of metal ions: said esterase is activated in the presence of 1 mM calcium ion, and inhibited in the presence of 1 mM cobalt ion, nickel ion, iron ion or ethylenediaminetetraacetic acid.
Claim 2
Dependent Claim
186 words
An essentially purified esterase derived from Serratia marcescens Sr41 (FERM BP-No. 487) having the following physico-chemical properties and enzymatic characteristics: (1) Activity: said esterase hydrolyzes an ester bond of organic carboxylates, (2) Substrate specificity: said esterase acts on alkyl esters of organic carboxylic acids, triglycerides or thiol esters, (3) Optimum pH: said esterase has an optimum pH of 7.5-9.0 when the hydrolysis is carried out using olive oil as the substrate, (4) pH stability: said esterase is stable at pH 5.0-9.0 when it is stored at 30° C. for one hour, (5) Optimum temperature: said esterase has an optimum temperature of 40°-50° C. when the hydrolysis is carried out using olive oil as the substrate, (6) Heat stability: said esterase is stable at a temperature of not higher than 50° C. when it is stored at pH 8.0 for 30 minutes, (7) Molecular weight: 62,000±2,000 (SDS-polyacrylamide gel electrophoresis), (8) Isoelectric point: 4.6±0.1, (9) Effect of metal ions: said esterase is activated in the presence of 1 mM calcium ion, and inhibited in the presence of 1 mM cobalt ion, nickel ion, iron ion or ethylenediaminetetraacetic acid.