Purification and characterisation of an ester hydrolase from a strain of Arthrobacter species: its application in asymmetrisation of 2-benzyl-1,3-propanediol acylates.
An ester hydrolase (ABL) has been isolated from a strain of Arthrobacter species (RRLJ-1/95) maintained in the culture collection of this laboratory. The purified enzyme has a specific activity of 1700 U/mg protein and is found to be composed of a single subunit (Mr 32,000), exhibiting both lipase and esterase activities shown by hydrolysis of triglycerides and p-nitrophenyl acetate respectively. Potential application of the enzyme concerns the asymmetrisation of prochiral 2-benzyl-1,3-propanediol esters besides enantioselective hydrolysis of alkyl esters of unsubstituted and substituted 1-phenyl ethanols.
Regional Research Laboratory (CSIR), Jammu-Tavwi, India.
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Johri
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Verma
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Parshad
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Koul
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Taneja
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Qazi
D001173:Arthrobacter / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009596:Nitrophenols / Q000378:metabolism; D020005:Propanols / Q000378:metabolism; D013237:Stereoisomerism; D014280:Triglycerides / Q000378:metabolism
D001426:Bacterial Proteins; D009596:Nitrophenols; D020005:Propanols; D014280:Triglycerides; C008642:4-nitrophenyl acetate; D002265:Carboxylic Ester Hydrolases; D008049:Lipase