Preparation of 3-deacetyl cephalosporins by Aspergillus niger lipase

Carrea, Giacomo; Corcelli, Alessandra; Palmisano, Giovanni; Riva, Sergio

doi:10.1002/(sici)1097-0290(19961220)52:6<648::aid-bit2>3.0.co;2-o

Cited by 14 publications

(6 citation statements)

References 11 publications

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“…Due to the high reactivity of the β-lactam ring, cephalosporin C is an ideal compound for mild and selective deacylation. Carrea et al screened 16 lipases for the 3-deacetylation of cephalosporin C (Scheme ) . Lipase from A. niger proved most efficient.…”

Section: Biotransformations With Eupergitmentioning

confidence: 99%

EUPERGIT Oxirane Acrylic Beads: How to Make Enzymes Fit for Biocatalysis

Böller

Meier

Menzler

2002

Org. Process Res. Dev.

161

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Enzyme recycling is essential for the development of large-scale enzyme-catalyzed biotransformations. Recycling is most convenient using enzymes immobilized on solid supports. Although immobilization on solid supports has been pursued since the 1950s, there are no general rules for selecting the best support for a given application. The commercial products EUPERGIT C and EUPERGIT C 250 L have been used for a wide variety of different enzymes and reactions. The present review draws up a comprehensive application profile of both EUPERGIT carriers. The reader gets (a) examples of biotransformations using oxidoreductases, transferases, hydrolases and lyases immobilized on EUPERGIT; (b) key data of the biotransformations, i.e., scale, yield, purity, and enantiomeric excess; (c) efficiency of the immobilization (% immobilized activity); (d) where appropriate, operational stability of the immobilized enzyme preparations, that is, number of cycles, residual activity; (e) specific advantages of the immobilized enzyme over the free enzyme apart from enzyme recycling, for example, improved stability and selectivity. Thus, the present review can serve as a guideline when selecting a resin for enzyme immobilization. Literature published between 1985 and 2000 is covered.

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Section: Biotransformations With Eupergitmentioning

confidence: 99%

EUPERGIT Oxirane Acrylic Beads: How to Make Enzymes Fit for Biocatalysis

Böller

Meier

Menzler

2002

Org. Process Res. Dev.

161

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“…These attractive features of lipases have developed considerable interest for their use in detergent (SARNEY and VULFSON 1995), surfactant (KIRAN et al 1999), leather (PANDEY et al 1999) and paper industries (JAEGER and REETZ 1998). They are also used in organic synthesis of fatty esters (ABBAS et al 2003), esterification reactions (NEGISHI et al 2003) and preparation of pharmaceuticals (DANIELI et al 1999) apart from their use in hydrolysis of fats and oils (CARREA et al 1996, CHOO et al 1998, CHOPINEAU et al 1988, CHRISTAKOPOULOS et al 1992. Several thermostable lipases exhibiting high activities have been characterized from micro-organisms such as yeast (BHUSHAN et al 1994), Bacillus thermocatenulatus (SCHMIDT-DANNERT et al 1994), Bacillus stearothermophilus L1 (KIM et al 1998), Bacillus sp.…”

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confidence: 99%

Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Sekhon

Dahiya

Tiwari

et al. 2005

J. Basic Microbiol.

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An extracellular lipase isolated from Bacillus megaterium AKG-1 had an optimum activity at 55 degrees C/pH 7.0. It retained 100% activity at 50 degrees C for 30 min with a half life of 30 min at 70 degrees C. A 20-70% increase in lipase activity was observed in presence of acetone (20% v/v), DMSO (20% v/v) and isopropanol (10% v/v). The enzyme activity was 92, 98 and 107% after 24 h, on treatment with 10% (v/v) acetone, benzene and isopropanol respectively. Deoxycholic acid, sodium deoxycholate, lithocholic acid, rhamnolipid, Brij 52 and cholic acid stimulated the lipase activity by 76, 36, 24, 24, 23.6 and 13%, respectively. Addition of reducing agents like sodium sulphite, sodium metabisulphite and L-cysteine-HCl, at 10 mM concentration stimulated lipase activity by 127, 146 and 150% respectively. The lipase appeared to show enantioselectivity in hydrolyzing racemic 3-acetoxy-beta-lactam as it hydrolyzed only the (+) enantiomer.

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“…El uso de esterasas para producir desacetilcefalosporinas fue primeramente demostrado con la acetil esterasas de la corteza de cítri-cos (Jeffrey et al, 1961). Posteriormente, otras esterasas y lipasas (Carrea et al, 1996) han sido publicadas y patentadas con la habilidad de desacetilar compuestos β-lactámicos. Entre los microorganismos donde ha sido encontrada esta actividad esterasa están Aureobasidium spp.…”

Section: • Síntesis De Antibióticos β-Lactámicosunclassified

Enzimas lipolíticas bacterianas: propiedades, clasificación, estructura, aplicaciones tecnológicas y aspectos legales

González¹,

Caston²

2012

Anales De Veterinaria De Murcia

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RESUMENLas enzimas lipolíticas son biocatalizadores que llevan a cabo reacciones de síntesis, hidrolisis o intercambios de grupos en sustancias oleosas. Las enzimas lipolíticas presentes en la naturaleza han sido utilizadas en la producción de alimentos durante millones de años, pero en las últimas décadas han adquirido una mayor importancia; debido a la multitud de aplicaciones tecnológicas en las que son capaces de actuar y a las ventajas que presentan frente a los catalizadores convencionales no biológicos. Una de las principales fuentes de estos biocatalizadores son las bacterias, ya que son fáciles y rápidas de cultivar, entre otras ventajas, y gracias a las técnicas de biología molecular pueden obtenerse en grandes cantidades. El objetivo de este trabajo es describir algunas de las aplicaciones industriales de las enzimas lipolíticas en las diferentes industrias, además, de hacer una breve reseña sobre sus propiedades generales, clasificación, mecanismo de actuación y el marco legal que las engloba.Palabras clave: enzimas alimentarias, procesado de alimentos, esterasas/lipasas.

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Preparation of 3-deacetyl cephalosporins by Aspergillus niger lipase

Cited by 14 publications

References 11 publications

EUPERGIT Oxirane Acrylic Beads: How to Make Enzymes Fit for Biocatalysis

EUPERGIT Oxirane Acrylic Beads: How to Make Enzymes Fit for Biocatalysis

Properties of a thermostable extracellular lipase from Bacillus megaterium AKG‐1

Enzimas lipolíticas bacterianas: propiedades, clasificación, estructura, aplicaciones tecnológicas y aspectos legales

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