Lipases: Interfacial Enzymes with Attractive Applications

Schmid, Rolf D.; Verger, Robert

doi:10.1002/(sici)1521-3773(19980703)37:12<1608::aid-anie1608>3.3.co;2-m

Cited by 228 publications

(329 citation statements)

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“…their ability to catalyze both hydrolysis and synthesis reactions with high regio-and enantioselectivity. Lipolytic enzymes have, therefore, developed into the most widely used class of enzymes in synthetic organic chemistry [13][14][15][16]. Consequently, the genes of many bacterial lipolytic enzymes have been identified, cloned, expressed and the corresponding enzymes have been characterized [17] which allowed the classification of more than 50 bacterial esterases and lipases into eight homology families [18].…”

Section: Introductionmentioning

confidence: 99%

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

Eggert

Pouderoyen

Pencreach

et al. 2002

Colloids and Surfaces B: Biointerfaces

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Section: Introductionmentioning

confidence: 99%

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

Eggert

Pouderoyen

Pencreach

et al. 2002

Colloids and Surfaces B: Biointerfaces

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“…A widely employed class of hydrolytic enzymes are lipases (EC 3.1.1.3) due to their high enantioselectivity, activity and stability, and their broad substrate specificity [1]. Chiral secondary alcohols are a well investigated class of substrates [2], which are converted in lipase catalyzed kinetic resolution through hydrolysis, esterification and transesterification.…”

Section: Introductionmentioning

confidence: 99%

Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols

Schulz¹,

Schmid²,

Pleiss³

2001

J Mol Model

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Lipases are widely applied catalysts for highly enantioselective resolution of chiral secondary alcohols. While stereopreference is determined predominantly by the substrate structure, stereoselectivity (enantioselectivity and diastereoselectivity) depends on atomic details of interactions between substrate and lipase. Experimentally (≤ 1.8 Å) for RR stereo isomers, which were also experimentally found to be hydrolyzed most rapidly; distances d(H Nε -O alc ) were about 2 Å for SS and SR stereo isomers, which were converted at similar rates but at lower rate than RR stereo isomers; finally, distances d(H Nε -O alc ) for SR stereo isomers were greater than 4 Å, in accordance with very slow conversion of SR stereo isomers.

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“…[1][2][3] Carboxylesterases (EC 3.1.1.1) and lipases (EC 3.1.1.3) are two major classes of esterases. Both enzymes are relatively stable in organic solvents 4) and have numerous applications in organic synthesis. They are useful catalysts for regio-and stereoselective reactions in fine-chemical synthesis, 3,5) and also used as bulk enzymes in a variety of chemical and other industries.…”

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confidence: 99%

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

Takehara

Kinoshita

Miyamoto

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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A novel esterase showing activity specific for esters of aryl-carboxylic acids was discovered in Sporosarcina sp. nov., which was identified by the 16S rDNA sequencing method in addition to morphological and physiological analyses. The aryl-carboxylesterase (named EstAC) was purified 780-fold from crude cell extracts by a 5-step procedure. EstAC was characterized as a monomeric protein with a molecular weight of 43,000, an optimum pH of around 9.0, and an optimum temperature of 40 C. The pH optimum and the effects of inhibitors together with an internal amino acid sequence suggested that EstAC is a member of family VIII esterases. EstAC was found to be highly active on a wide variety of substrates such as alkyl benzoates, alkyl phenylacetates, ethyl -or -substituted phenylpropionates, dialkyl terephthalates, dimethyl isophthalate, and ethylene glycol dibenzoate. However, monomethyl terephthalate was not hydrolyzed. It was suggested that EstAC had 4-hydroxybenzoyl and cinnamoyl esterase activities as well.

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Lipases: Interfacial Enzymes with Attractive Applications

Cited by 228 publications

References 0 publications

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols

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

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