Biotransformation of (−)β-Pinene by Aspergillus niger ATCC 9642

Toniazzo, Geciane; Oliveira, Débora de; Dariva, Cláudio; Oestreicher, Enrique G.; Antunes, O. A. C.

doi:10.1007/978-1-59259-991-2_71

Cited by 15 publications

(20 citation statements)

References 14 publications

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“…Where as biotransformation of (-)-a-Pinene produced 28.146 ± 0.65 mg of a-Terpineol and 9.774 ± 1.44 mg of isoterpineol at the end of 72 h. The results obtained in this work indicate that the enzymes responsible for the biotransformation producing the metabolites found in all the reaction systems studied are probably not having stereoselectivity, since the bioconversions of both the substrates resulted in the production of same compounds. Aspergillus niger selectively transformed a-pinene to verbenone, verbenol and a-terpineol whereas b-pinene to only a-terpineol [12,13]. The biotransformation of (-)-a-Pinene and (?…”

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confidence: 99%

Biotransformation of α-Pinene to Terpineol by Resting Cell Suspension of Absidia corulea

et al. 2011

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Microbial biotransformation of monoterpenes results in the formation of many valuable compounds. Many microorganisms can be used to carry out extremely specific conversions using substrates of low commercial value. Absidia corulea MTCC 1335 was examined for its ability to transform a-Pinene enantiomers. The substrates (-)-a-Pinene and (?)-a-Pinene converted to a-terpineol and isoterpineol, were detected in gas chromatographic analysis. The Biotransformation kinetics of the oxidized products were analysed using GC-MS. With both the substrates the products formed were similar and not much difference in the rate of transformation was observed, suggesting no enantioselectivity of organism towards the substrate.

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confidence: 99%

Biotransformation of α-Pinene to Terpineol by Resting Cell Suspension of Absidia corulea

et al. 2011

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“…Reduction (Medina, Stefani and Brandelli, 2006;Lacerda et al, 2006a;Lacerda et al, 2006b;Ribeiro et al, 2006), Hydrolysis (Wang et al, 2006); Oxidation (Rozenbaum et al, 2006;Durand et al, 2006;Toniazzo et al, 2006;Toniazzo et al, 2005;Santos et al, 2004;Santos et al, 2003) and other chemical transformations (Xie and West, 2006;Paggy, Rodriguez and Fay, 2005) have been successfully undertaken by several groups.…”

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confidence: 99%

Production of enantiomerically pure D-Phenylglycine using Pseudomonas aeruginosa 10145 as biocatalyst

Alonso¹,

Oestreicher²,

Antunes³

2008

Braz. J. Chem. Eng.

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-Different bacterial strains were screened to detect nitrilase and/or nitrile hidratase/amidase activities towards benzonitrile, to be used as biocatalyst to produce enantiomerically pure non-proteinogenic amino acids using amino nitriles as starting material. The best biocatalyst found was Pseudomonas aeruginosa 10145, which showed high enzyme activities. Whole cells were used as catalyst for the transformation of 2-phenyl-2-amino-acetonitrile for the corresponding D-phenylglycine. The percentage conversion was followed by chiral HPLC. After 1 hour reaction 18% of 2-phenyl-2-amino-acetonitrile was converted into D-phenylglycine with an enantiomeric excess of over 95%. When an inducer was added to the media, an increase in nitrile hydrolyzing activities was detected, hence leading to total conversion of (R)-2-phenyl-2-amino-acetonitrile to the corresponding amino acid in 30 min reaction. The isolated yield of the target product was 50% and its characterization was performed by polarimetry, chiral HPLC, IR-FT spectroscopy and GC-MS.

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“…ionic liquids, supercritical fluids) and physical stabilization (e.g. immobilization, CLEAS) have been developed, which in combination are powerful tools to improve biotransformation and to synthesize new products [13], [14]. In this study, relevant results of the epoxidation of α-pinene and peroxycarboxylic acids using lipase from p. aeruginosa was presented.…”

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Lipase-Mediated Formation of Peroxyoctanoic Acid Used in Catalytic Epoxidation of α-Pinene from Turpentine Oil

Wijayati¹,

Siadi²,

Wijaya³

et al. 2015

IJCEA

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Abstract-This work describes the lipase-mediated synthesis of α -pinene oxide at ambient temperature. The immobilized lipase from Pseudomonas aeruginosa is used to generate peroxyoctanoic acid directly from octanoic acid and hydrogen peroxide. The peroxy acid formed is then applied for in situ oxidation of α -pinene. High conversion of α -pinene to α -pinene oxide (approximately 78%) was achieved when using 0,1 g enzim lipase, 6 mmol H 2 O 2 , dan 5 mmol octanoic acid. Various parameters affecting the conversion of α -pinene to α -pinene oxide were studied Index Terms-α-Pinene, P. aeruginosa, octanoic acid.

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Biotransformation of (−)β-Pinene by Aspergillus niger ATCC 9642

Cited by 15 publications

References 14 publications

Biotransformation of α-Pinene to Terpineol by Resting Cell Suspension of Absidia corulea

Biotransformation of α-Pinene to Terpineol by Resting Cell Suspension of Absidia corulea

Production of enantiomerically pure D-Phenylglycine using Pseudomonas aeruginosa 10145 as biocatalyst

Lipase-Mediated Formation of Peroxyoctanoic Acid Used in Catalytic Epoxidation of α-Pinene from Turpentine Oil

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