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Special Issue "Organic Synthesis Using Biocatalyst"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Green Chemistry".

Deadline for manuscript submissions: closed (31 August 2012)

Special Issue Editor

Guest Editor
Prof. Dr. Tomoko Matsuda (Website)

Tokyo Institute of Technology, Graduate School of Bioscience and Biotechnology, Department of Bioengineering, 4259 Nagatsuta, Midori-ku, Yokohama, 226-850, Japan
Phone: +81-45-924-5757

Special Issue Information

Dear Colleagues,

Organic synthesis using biocatalysts, especially chiral synthesis, is increasingly getting important for variety of purposes such as drug synthesis and total synthesis due to the high chemo-, region-, and enantio-selectivities of enzyme. More than half of drug candidate molecules have more than one chiral centers and about 10% of the total drug synthesis depends on the biocatalyst. Importantly, these successes are owing to achievements of basic researches. Therefore, this special issue will present novel, unique and innovative application research as well as basic research concerning organic synthesis using biocatalysts. I also hope that this issue will contribute for green chemistry since the enzyme is a natural and reproducible catalyst with high efficiency.

Dr. Tomoko Matsuda
Guest Editor

Keywords

  • chiral synthesis
  • total synthesis
  • novel biocatalyst for organic synthesis
  • green chemistry

Published Papers (5 papers)

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Research

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Open AccessArticle Production of (R)-3-Quinuclidinol by E. coli Biocatalysts Possessing NADH-Dependent 3-Quinuclidinone Reductase (QNR or bacC) from Microbacterium luteolum and Leifsonia Alcohol Dehydrogenase (LSADH)
Int. J. Mol. Sci. 2012, 13(10), 13542-13553; doi:10.3390/ijms131013542
Received: 30 August 2012 / Revised: 27 September 2012 / Accepted: 11 October 2012 / Published: 19 October 2012
Cited by 5 | PDF Full-text (320 KB) | HTML Full-text | XML Full-text
Abstract
We found two NADH-dependent reductases (QNR and bacC) in Microbacterium luteolum JCM 9174 (M. luteolum JCM 9174) that can reduce 3-quinuclidinone to optically pure (R)-(−)-3-quinuclidinol. Alcohol dehydrogenase from Leifsonia sp. (LSADH) was combined with these reductases to regenerate NAD [...] Read more.
We found two NADH-dependent reductases (QNR and bacC) in Microbacterium luteolum JCM 9174 (M. luteolum JCM 9174) that can reduce 3-quinuclidinone to optically pure (R)-(−)-3-quinuclidinol. Alcohol dehydrogenase from Leifsonia sp. (LSADH) was combined with these reductases to regenerate NAD+ to NADH in situ in the presence of 2-propanol as a hydrogen donor. The reductase and LSADH genes were efficiently expressed in E. coli cells. A number of constructed E. coli biocatalysts (intact or immobilized) were applied to the resting cell reaction and optimized. Under the optimized conditions, (R)-(−)-3-quinuclidinol was synthesized from 3-quinuclidinone (15% w/v, 939 mM) giving a conversion yield of 100% for immobilized QNR. The optical purity of the (R)-(−)-3-quinuclidinol produced by the enzymatic reactions was >99.9%. Thus, E. coli biocatalysis should be useful for the practical production of the pharmaceutically important intermediate, (R)-(−)-3-quinuclidinol. Full article
(This article belongs to the Special Issue Organic Synthesis Using Biocatalyst)
Open AccessArticle Optimization of Lipase-Mediated Synthesis of 1-Nonene Oxide Using Phenylacetic Acid and Hydrogen Peroxide
Int. J. Mol. Sci. 2012, 13(10), 13140-13149; doi:10.3390/ijms131013140
Received: 27 July 2012 / Revised: 1 September 2012 / Accepted: 21 September 2012 / Published: 12 October 2012
Cited by 4 | PDF Full-text (441 KB) | HTML Full-text | XML Full-text
Abstract
Herein, an efficient epoxidation of 1-nonene is described. In a simple epoxidation system, commercially available Novozym 435, an immobilized Candida antarctica lipase B, and hydrogen peroxide (H2O2) were utilized to facilitate the in situ oxidation of phenylacetic acid [...] Read more.
Herein, an efficient epoxidation of 1-nonene is described. In a simple epoxidation system, commercially available Novozym 435, an immobilized Candida antarctica lipase B, and hydrogen peroxide (H2O2) were utilized to facilitate the in situ oxidation of phenylacetic acid to the corresponding peroxy acid which then reacted with 1-nonene to give 1-nonene oxide with high yield and selectivity. The aliphatic terminal alkene was epoxidised efficiently in chloroform to give an excellent yield (97%–99%) under the optimum reaction conditions, including temperature (35 °C), initial H2O2 concentration (30%), H2O2 amount (4.4 mmol), H2O2 addition rate (one step), acid amount (8.8 mmol), and stirring speed (250 rpm). Interestingly, the enzyme was stable under the single-step addition of H2O2 with a catalytic activity of 190.0 Ug−1. The entire epoxidation process was carried out within 12 h using a conventional water bath shaker. Full article
(This article belongs to the Special Issue Organic Synthesis Using Biocatalyst)
Figures

Open AccessArticle Combination of Oxyanion Gln114 Mutation and Medium Engineering to Influence the Enantioselectivity of Thermophilic Lipase from Geobacillus zalihae
Int. J. Mol. Sci. 2012, 13(9), 11666-11680; doi:10.3390/ijms130911666
Received: 25 May 2012 / Revised: 10 August 2012 / Accepted: 20 August 2012 / Published: 17 September 2012
Cited by 7 | PDF Full-text (522 KB) | HTML Full-text | XML Full-text
Abstract
The substitution of the oxyanion Q114 with Met and Leu was carried out to investigate the role of Q114 in imparting enantioselectivity on T1 lipase. The mutation improved enantioselectivity in Q114M over the wild-type, while enantioselectivity in Q114L was reduced. The enantioselectivity of the thermophilic lipases, T1, Q114L and Q114M correlated better with log p as compared to the dielectric constant and dipole moment of the solvents. Enzyme activity was good in solvents with log p < 3.5, with the exception of hexane which deviated substantially. Isooctane was found to be the best solvent for the esterification of (R,S)-ibuprofen with oleyl alcohol for lipases Q114M and Q114L, to afford E values of 53.7 and 12.2, respectively. Selectivity of T1 was highest in tetradecane with E value 49.2. Solvents with low log p reduced overall lipase activity and dimethyl sulfoxide (DMSO) completely inhibited the lipases. Ester conversions, however, were still low. Molecular sieves employed as desiccant were found to adversely affect catalysis in the lipase variants, particularly in Q114M. The higher desiccant loading also increased viscosity in the reaction and further reduced the efficiency of the lipase-catalyzed esterifications. Full article
(This article belongs to the Special Issue Organic Synthesis Using Biocatalyst)
Open AccessArticle Biosysthesis of Corn Starch Palmitate by Lipase Novozym 435
Int. J. Mol. Sci. 2012, 13(6), 7226-7236; doi:10.3390/ijms13067226
Received: 23 April 2012 / Revised: 12 May 2012 / Accepted: 23 May 2012 / Published: 12 June 2012
Cited by 14 | PDF Full-text (412 KB) | HTML Full-text | XML Full-text
Abstract
Esterification of starch was carried out to expand the usefulness of starch for a myriad of industrial applications. Lipase B from Candida antarctica, immobilized on macroporous acrylic resin (Novozym 435), was used for starch esterification in two reaction systems: micro-solvent system [...] Read more.
Esterification of starch was carried out to expand the usefulness of starch for a myriad of industrial applications. Lipase B from Candida antarctica, immobilized on macroporous acrylic resin (Novozym 435), was used for starch esterification in two reaction systems: micro-solvent system and solvent-free system. The esterification of corn starch with palmitic acid in the solvent-free system and micro-solvent system gave a degree of substitution (DS) of 1.04 and 0.0072 respectively. Esterification of corn starch with palmitic acid was confirmed by UV spectroscopy and IR spectroscopy. The results of emulsifying property analysis showed that the starch palmitate with higher DS contributes to the higher emulsifying property (67.6%) and emulsion stability (79.6%) than the native starch (5.3% and 3.9%). Modified starch obtained by esterification that possesses emulsifying properties and has long chain fatty acids, like palmitic acid, has been widely used in the food, pharmaceutical and biomedical applications industries. Full article
(This article belongs to the Special Issue Organic Synthesis Using Biocatalyst)

Review

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Open AccessReview Biotransformations Utilizing β-Oxidation Cycle Reactions in the Synthesis of Natural Compounds and Medicines
Int. J. Mol. Sci. 2012, 13(12), 16514-16543; doi:10.3390/ijms131216514
Received: 31 August 2012 / Revised: 19 November 2012 / Accepted: 21 November 2012 / Published: 5 December 2012
Cited by 6 | PDF Full-text (3412 KB) | HTML Full-text | XML Full-text
Abstract
β-Oxidation cycle reactions, which are key stages in the metabolism of fatty acids in eucaryotic cells and in processes with a significant role in the degradation of acids used by microbes as a carbon source, have also found application in biotransformations. One [...] Read more.
β-Oxidation cycle reactions, which are key stages in the metabolism of fatty acids in eucaryotic cells and in processes with a significant role in the degradation of acids used by microbes as a carbon source, have also found application in biotransformations. One of the major advantages of biotransformations based on the β-oxidation cycle is the possibility to transform a substrate in a series of reactions catalyzed by a number of enzymes. It allows the use of sterols as a substrate base in the production of natural steroid compounds and their analogues. This route also leads to biologically active compounds of therapeutic significance. Transformations of natural substrates via β-oxidation are the core part of the synthetic routes of natural flavors used as food additives. Stereoselectivity of the enzymes catalyzing the stages of dehydrogenation and addition of a water molecule to the double bond also finds application in the synthesis of chiral biologically active compounds, including medicines. Recent advances in genetic, metabolic engineering, methods for the enhancement of bioprocess productivity and the selectivity of target reactions are also described. Full article
(This article belongs to the Special Issue Organic Synthesis Using Biocatalyst)

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