Enzyme immobilization utilizing a porous ceramics support for chiral synthesis

Kamori, Masanobu; Yamashita, Yoshitaka; Naoshima, Yoshinobu

doi:10.1002/chir.10085

Cited by 11 publications

(7 citation statements)

References 12 publications

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“…1) of the forward and reverse reactions for the transesterification of (R)-1-phenylethanol with vinyl acetate as acyl donor catalyzed by CALB immobilized on fumed silica in hexane indicates that our experimental and analytical procedures appear consistent. Comparison with the literature confirms this in hexane (Sriappareddy et al, 2007) and other organic solvents (Han et al, 2006;Kamori et al, 2002).…”

Section: Resultssupporting

confidence: 70%

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Kramer

Cruz

Pfromm

et al. 2010

Journal of Biotechnology

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Enzymatic catalysis to produce molecules such as perfumes, flavors, and fragrances has the advantage of allowing the products to be labeled "natural" for marketing in the U.S., in addition to the exquisite selectivity and stereoselectivity of enzymes that can be an advantage over chemical catalysis. Enzymatic catalysis in organic solvents is attractive if solubility issues of reactants or products, or thermodynamic issues (water as a product in esterification) complicate or prevent aqueous enzymatic catalysis. Immobilization of the enzyme on a solid support can address the generally poor solubility of enzymes in most solvents.We have recently reported on a novel immobilization method for Candida antarctica Lipase B on fumed silica to improve the enzymatic activity in hexane. This research is extended here to study the enantioselective transesterification of (RS)-1-phenylethanol with vinyl acetate. The maximum catalytic activity for this preparation exceeded the activity (on an equal enzyme amount basis) of the commercial Novozyme 435® significantly. The steady-state conversion for (R)-1-phenylethanol was about 75% as confirmed via forward and reverse reaction. The catalytic activity steeply increases with increasing nominal surface coverage of the support until a maximum is reached at a nominal surface coverage of 230%. We hypothesize that the physical state of the enzyme molecules at a low surface coverage is dominated in this case by detrimental strong enzyme-substrate interactions. Enzyme-enzyme interactions may stabilize the active form of the enzyme as surface coverage increases while diffusion limitations reduce the apparent catalytic performance again at multi-layer coverage. The temperature-, solvent-, and long-term stability for CALB/fumed silica preparations showed that these preparations can tolerate temperatures up to 70°C, continuous exposure to solvents, and long term storage.2

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Section: Resultssupporting

confidence: 70%

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Kramer

Cruz

Pfromm

et al. 2010

Journal of Biotechnology

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“…Our group has investigated the enantioselectivity of such enzyme lipases as Burkholderia cepacia lipase (BCL) and Candida antarctica lipase typeB (CALB) through their biocatalytic synthetic reactions with lipases [1][2][3][4][5]. The degree of enantioselectivity is given by an experimentally obtained E value that is an enantiomeric ratio for each lipase-catalyzed reaction [6].…”

Section: Introductionmentioning

confidence: 99%

Biomolecular Chemical Simulations toward Elucidation of the Enantioselectivity and Reactivity of Lipases in Organic Synthesis

Yagi

Kimura²,

Kamezawa³

et al. 2018

CBIJ

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We are presently continuing to perform biomolecular chemical simulations for Burkholderia cepacia lipase (BCL) and Candida antarctica lipase typeB (CALB) to predict their enantioselectivity and reactivity toward various organic compounds. Here, we describe molecular dynamics (MD) and fragment molecular orbital (FMO) calculations on the complexes of CALB with primary and secondary alcohol esters. For esters with high enantioselectivity, the fast-reacting enantiomer of esters is located near the active site of CALB, whereas the slow-reacting enantiomer of esters moves away from the active site of CALB. On the other hand, for the esters with low enantioselectivity, we found that both (R)-and (S)-enantiomers of esters remain the active site of CALB. The FMO computations indicate that for the esters with high enantioselectivity, each fast-reacting enantiomer shows strong interactions with some particular amino acid residues, including Thr40, whereas for the esters with low enantioselectivity, both (R)-and (S)-enantiomers interact with identical amino acid residues including Thr40. It is predictable that Thr40 in CALB plays an important role in the chiral recognition of enantiomers through lipase-catalyzed biotransformations.

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“…The degree of the enantioselectivity, however, has to be elucidated by experimental work. Our interest has been focused on the lipase-catalysed enantioselective and clean synthesis of biologically important chiral compounds and on the control of the stereoselectivity and specificity [4][5][6][7][8]. As part of our continuous works toward conducting biocatalytic synthetic reactions with lipases, we aimed at understanding the enantioselectivity of enzyme lipases such as Burkholderia cepacia lipase (BCL) and Candida antarctica lipase typeB (CALB) through the combination of experimental chemistry and computational simulation [9][10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Large-Scale Biomolecular Chemical Computations toward the Prediction of Burkholderia cepacia Lipase Enantioselectivity

Yagi

Tanaka

Imagawa

et al. 2014

JASSE

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We have performed the molecular dynamics (MD) and the fragment molecular orbital (FMO) calculations on the complexes of Burkholderia cepacia lipase (BCL) with alcohol esters toward the prediction of lipase enantioselectivity. The MD computations show that for esters of high enantioselectivity, the difference in the CO interatomic distance between (R)-and (S)-enantiomer complexes is more than 9.0Å, while for esters of low enantioselectivity, the difference is less than 3.0Å. In addition, the FMO computations indicate that for the esters with high enantioselectivity, each fast reacting enantiomer shows strong interactions with some particular amino acids including HIS286 in BCL, whereas for esters with low enantioselectivity, both (R)-and (S)-enantiomers interact with the identical amino acids including HIS286.

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Enzyme immobilization utilizing a porous ceramics support for chiral synthesis

Cited by 11 publications

References 12 publications

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

<b>Biomolecular Chemical Simulations toward Elucidation of the Enantioselectivity and Reactivity of Lipases in Organic Synthesis</b><b> </b>

Large-Scale Biomolecular Chemical Computations toward the Prediction of <i>Burkholderia cepacia</i> Lipase Enantioselectivity

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