Kinetic resolutions with novel, highly enantioselective fungal lipases produced by solid state fermentation

Nagy, Viviána; Tőke, Enikő R.; Lee, Chee Keong; Szatzker, Gábor; Demirtaş, İbrahim; Omar, Ibrahim Che; Szakács, George; Poppe, László

doi:10.1016/j.molcatb.2006.01.012

Cited by 52 publications

(33 citation statements)

References 41 publications

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“…as reported by Bigey et al [37]; from Mucor mucedo by Stern et al [38] and Mucor sp. by Abbas et al [39]; from Scopulariopsis brevicaulis by Nagy et al [40] which was able to resolve racemic 1-phenylethanol rac-1a and racemic 1-cyclohexylethanol rac-1b displaying its biocatalytic activity and enantiomer selectivity; and from Aureobasidium pullulans by Leathers et al [41]. As shown in Table 1, Strain C3 (Rhizopus oryzae) had the highest lipase activity.…”

Section: Resultsmentioning

confidence: 99%

Studies on the Optimization of Lipase Production by Rhizopus sp. ZAC3 Isolated from the Contaminated Soil of a Palm Oil Processing Shed

Ayinla¹,

Ademakinwa²,

Agboola³

2017

J App Biol Biotech

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This study investigated the screening, production and optimization of an extracellular lipase from a fungus isolated from the contaminated soil of a palm oil processing shed. This was with a view to obtaining a strain that can secrete lipase with biochemical properties exploitable for biotechnological applications such as bioremediation of oil contaminated sites. Soil samples were collected from palm oil contaminated sites in Gbogan, Osun State, Nigeria (Latitude N 7°29.1481´ and Longitude E 4°20.7587´). The isolated fungal strains were screened on tributyrin agar for exogenous lipolytic activity. Molecular identification was carried out by amplifications of ITS-1, 5.8S and ITS-2 regions. The effects of incubation time, inducers, pH, temperature, carbon and nitrogen sources were varied for optimal lipase production using one factor at a time approach. Rhizopus oryzae ZAC3 (NCBI accession No: KX035094) was identified as the highest lipaseproducing strain. Maximum lipase production was observed on the fourth day, pH 5.0 and a temperature of 45 o C. Olive oil, xylose and yeast extract were the best inducer, carbon and nitrogen sources respectively for lipase production. There was a 2.02 fold increase in lipase production under these optimized conditions. In conclusion, Rhizopus oryzae ZAC3 lipase has properties exploitable for industrial and biotechnological applications.

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Section: Resultsmentioning

confidence: 99%

Studies on the Optimization of Lipase Production by Rhizopus sp. ZAC3 Isolated from the Contaminated Soil of a Palm Oil Processing Shed

Ayinla¹,

Ademakinwa²,

Agboola³

2017

J App Biol Biotech

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“…From our previous screens of thermophilic (SmF) 6 and mesophilic filamentous fungi (SSF), 7 several biocatalysts having comparable lipase activities and enantiomer selectivities to the widely used commercially available lipases were available for further screening.Within the strains of the SSF screen, 7 a preparation (Mucor hiemalis) with the less usual anti-Kazlauskas selectivity was also found. Therefore we could study the kinetic resolution of several less characterized racemic allylic alcohols by a range of commercial and in-house prepared enzymes.…”

Section: Resultsmentioning

confidence: 99%

“…5 The commercial availability of a range of lipase preparations at low cost has also widely expanded their use as biocatalysts in organic chemistry. Several studies on screening some thermophilic filamentous fungi in submerged fermentation (SmF) conditions, 6 and some poorly studied mesophilic fungi in solid state fermentation (SSF) 7 conditions for lipase/esterase activity resulted in biocatalysts exhibiting high enantiomer selectivity in synthetic biotransformations. The recent study of fungal SSF preparations acting on several typical secondary alcohols − such as 1-phenylethanol, 1-cyclohexylethanol and 1-(napth-2-yl)ethanol − as model substrates indicated that SSF biocatalysts with lipase activity are applicable in kinetic resolutions of racemic secondary alcohols.…”

Section: Introductionmentioning

confidence: 99%

“…The recent study of fungal SSF preparations acting on several typical secondary alcohols − such as 1-phenylethanol, 1-cyclohexylethanol and 1-(napth-2-yl)ethanol − as model substrates indicated that SSF biocatalysts with lipase activity are applicable in kinetic resolutions of racemic secondary alcohols. 7 As the gently dried SSF preparations do not require costly downstream processes, they can be considered as inexpensive, naturally immobilized biocatalysts. In the enzyme-catalyzed acetylation of the three selected racemic secondary alcohols 7 several of the SSF biocatalysts exhibited high but usual enantioselectivities [formation of the (R)-acetates] according to the so-called "Kazlauskas' rule", 8 whereas one strain (Mucor hiemalis) resulted in a selective "anti-Kazlauskas" biocatalyst by SSF.…”

Section: Introductionmentioning

confidence: 99%

“…In the enzyme-catalyzed acetylation of the three selected racemic secondary alcohols 7 several of the SSF biocatalysts exhibited high but usual enantioselectivities [formation of the (R)-acetates] according to the so-called "Kazlauskas' rule", 8 whereas one strain (Mucor hiemalis) resulted in a selective "anti-Kazlauskas" biocatalyst by SSF. 7 As the secondary alcohols in this study (with SSF biocatalysts) contained rigid (aromatic) or more flexible (cyclohexane) ring adjacent to the asymmetric carbon centre, 7 one of our aims was to broaden the selection of the substrates for these SSF preparations by studying the kinetic resolution of allylic alcohols containing the rings at more remote position from the asymmetric center. The enantiomerically pure forms of such allylic alcohols (4-aryl-and 4-heteroarylsubstituted but-3-en-2-ols) and acetates are useful synthons which can be transformed to a wide range of more complex molecules.…”

Section: Introductionmentioning

confidence: 99%

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Lipase-catalyzed kinetic resolution of 4-aryl- and 4-heteroarylbut-3-en-2-ols

Szigeti¹,

Tőke²,

Turoczi³

et al. 2007

Arkivoc

Self Cite

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Several 4-aryl-and 4-heteroarylbut-3-en-2-ones [2a-c, bearing 4-phenyl-, 4-(furan-2-yl)-and 4-(1-benzyl-1H-indol-3yl)-substituents, respectively] were prepared by condensation reaction of acetone with the corresponding aldehydes (1a-c). Reduction of the ketones (2a,b) with NaBH 4 resulted in the formation of the corresponding racemic secondary alcohols (rac-3a,b). On the other hand, reduction of the ketone bearing indole moiety (2c) gave an unstable product. The lipase-catalyzed enantiomer selective acetylation of the alcohols (rac-3a,b) by vinyl acetate has been investigated with a crude lipase from submerged fermentation (SmF) of a thermophilic fungus, with several crude enzyme preparations from solid state fermentation (SSF) of selected mesophilic fungi and with several commercially available lipases. The commercial and SmF lipases and the majority of SSF preparations exhibited high but usual enantiomer selectivities and resulted in the formation of (R)-acetates [(R)-4a,b] according to the Kazlauskas' rule. Several SSF preparations, however, behaved as selective anti-Kazlauskas catalysts.

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Efficient kinetic resolution of (RS)‐1‐phenylethanol by a mycelium‐bound lipase from a wild‐type Aspergillus oryzae strain

Yan

Zhao

Qian

2016

Biotech and App Biochem

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A mycelium-bound lipase from Aspergillus oryzae (AOL) exhibited excellent enantioselectivity for kinetic resolution of (RS)-1-phenylethanol ((RS)-1-PE) in organic solvent. The various reaction parameters affecting the conversion and enantioselectivity were studied, including type of acyl donor, solvent, molar ratio, temperature, enzyme amount, and substrate concentration. The optimum reaction conditions were found to be transesterification with vinyl acetate at 30 °C in methyl tert-butyl ether with a vinyl acetate: (RS)-1-PE molar ratio of 1:1 and an enzyme concentration of 60 g/L. At the optimum reaction conditions, the conversion could reach above 46% with >99% enantiomeric excess of the product, (R)-1-phenylethyl acetate, when the substrate concentration was below 1.4 M. The enzyme displayed an excellent enantioselectivity with an E-value of >200 and a strong tolerance for high substrate concentration of up to 1.8 M. Those results indicated that AOL was a promising biocatalyst in the kinetic resolution of (RS)-1-PE.

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Kinetic resolutions with novel, highly enantioselective fungal lipases produced by solid state fermentation

Cited by 52 publications

References 41 publications

Studies on the Optimization of Lipase Production by Rhizopus sp. ZAC3 Isolated from the Contaminated Soil of a Palm Oil Processing Shed

Studies on the Optimization of Lipase Production by Rhizopus sp. ZAC3 Isolated from the Contaminated Soil of a Palm Oil Processing Shed

Lipase-catalyzed kinetic resolution of 4-aryl- and 4-heteroarylbut-3-en-2-ols

Efficient kinetic resolution of (RS)‐1‐phenylethanol by a mycelium‐bound lipase from a wild‐type Aspergillus oryzae strain

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