Syntheses of Enantiopure Aliphatic Secondary Alcohols and Acetates by Bioresolution with Lipase B from Candida antarctica

Ferreira, Hercules V.; Rocha, Lenilson C.; Severino, Richele P.; Porto, André Luiz Meleiro

doi:10.3390/molecules17088955

Cited by 29 publications

(21 citation statements)

References 29 publications

(35 reference statements)

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“…Enzyme mediated kinetic resolution of such alcohols using lipases, esterases, and alcohol dehydrogenases have been reported in the literature. [9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28] For example, resolution of (±)-lavandulol has been achieved previously with various lipases such as Candida antarctica lipase B (CAL B), 9 Hog pancreas lipase, 29 Porcine pancreas lipase, 26 and Yarrowia lipolytica lipases. 30 However, enzyme catalyzed resolution process is associated with several disadvantages such as higher cost, low substrate concentration, instability and cofactor dependency of the enzymes in several occasions.…”

Section: Introductionmentioning

confidence: 99%

Fungal mediated kinetic resolution of racemic acetates to ( R )-alcohols using Fusarium proliferatum

Jadhav

Patil

Chaya

et al. 2016

Tetrahedron Letters

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Section: Introductionmentioning

confidence: 99%

Fungal mediated kinetic resolution of racemic acetates to ( R )-alcohols using Fusarium proliferatum

Jadhav

Patil

Chaya

et al. 2016

Tetrahedron Letters

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“…Since de novo design is not a totally new idea, similar idea had been used in drug design for years such as LUDI, SPOUT . However, these programs are designed to build an inhibitor, which is a ‘sticky’ molecule that could efficiently bind to enzyme and probably suppress or destroy the catalytic activities, in order to find target molecules for new drugs.…”

Section: Discussionmentioning

confidence: 99%

Crius: A novel fragment‐based algorithm of de novo substrate prediction for enzymes

et al. 2018

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The study of enzyme substrate specificity is vital for developing potential applications of enzymes. However, the routine experimental procedures require lot of resources in the discovery of novel substrates. This article reports an in silico structure-based algorithm called Crius, which predicts substrates for enzyme. The results of this fragment-based algorithm show good agreements between the simulated and experimental substrate specificities, using a lipase from Candida antarctica (CALB), a nitrilase from Cyanobacterium syechocystis sp. PCC6803 (Nit6803), and an aldo-keto reductase from Gluconobacter oxydans (Gox0644). This opens new prospects of developing computer algorithms that can effectively predict substrates for an enzyme.

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“…CALB is one of the most employed enzymes in biocatalysis by virtue of its catalytic versatility, thermostability, and excellent regio‐ and enantioselectivity . Many reports in the literature illustrate the ability of CALB to perform synthesis, hydrolysis, alcoholysis, acidolysis, acetylation, deacetylation, and transesterification reactions of a wide range of substrates such as primary and secondary alcohols, polymers, chiral carboxylic acids, chiral alcohols, and amines …”

Section: Introductionmentioning

confidence: 99%

Cross‐linked enzyme aggregates of recombinant Candida antarctica lipase B for the efficient synthesis of olvanil, a nonpungent capsaicin analogue

Diaz‐Vidal

Armenta‐Perez

Navarro-Partida

et al. 2019

Biotechnology Progress

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Despite the proven therapeutic role of capsaicin in human health, its usage is still hampered by its high pungency. In this sense, nonpungent capsaicin analogues as olvanil are a feasible alternative to the unpleasant sensations produced by capsaicin while maintaining a similar pharmacological profile. Olvanil can be obtained by a lipase‐catalyzed chemoenzymatic process. In the present work, recombinant Candida antarctica lipase B (CALB) was expressed in Pichia pastoris and subsequently immobilized by cross‐linked enzyme aggregate (CLEA) methodology for the synthesis of olvanil. The CALB‐CLEAs were obtained directly from the fermentation broth of P. pastoris without any purification step in order to assess the role of the contaminant proteins of the crude extract as co‐feeders. The CALB‐CLEAs were also bioimprinted to enhance the catalytic performance in olvanil synthesis. When CALB was precipitated with isopropanol, the obtained CALB‐CLEAs exhibited the highest activity in the synthesis of olvanil, regardless of the glutaraldehyde concentration. The maximum product synthesis was found at 72 hr obtaining 6.8 g L−1 of olvanil with a reaction yield of 16%. When CALB was bioimprinted with olvanil, the synthesis was enhanced 1.3 times, reaching 10.7 g L−1 of olvanil at 72 hr of reaction with a reaction yield of 25%. Scanning electron microscopy images indicated different morphologies of the CLEAs depending on the precipitating agent and the template used for bioimprinting. Recombinant CALB‐CLEAs obtained directly from the fermentation broth are a suitable alternative to commercial enzymatic preparations for the synthesis of olvanil in organic medium.

show abstract

Syntheses of Enantiopure Aliphatic Secondary Alcohols and Acetates by Bioresolution with Lipase B from Candida antarctica

Cited by 29 publications

References 29 publications

Fungal mediated kinetic resolution of racemic acetates to ( R )-alcohols using Fusarium proliferatum

Fungal mediated kinetic resolution of racemic acetates to ( R )-alcohols using Fusarium proliferatum

Crius: A novel fragment‐based algorithm of de novo substrate prediction for enzymes

Cross‐linked enzyme aggregates of recombinant Candida antarctica lipase B for the efficient synthesis of olvanil, a nonpungent capsaicin analogue

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