Enantiopreference of Candida antarctica lipase B toward carboxylic acids: Substrate models and enantioselectivity thereof

Tsai, Shau‐Wei

doi:10.1016/j.molcatb.2014.07.010

Cited by 34 publications

(16 citation statements)

References 212 publications

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“…The parameters ( ee p and ee s ) were calculated according the integrated area of the enantiomers. The absolute configuration was determined by comparison with data previously reported for these enzymes …”

Section: Methodsmentioning

confidence: 99%

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Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

et al. 2017

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The application of several immobilized lipases has been explored in the enantioselective esterification of (R,S)-2-methylbutyric acid, an insect pheromone precursor. With the use of Candida antarctica B, using hexane as solvent, (R)-pentyl 2-methylbutyrate was prepared in 2 h with c 40%, ee p 90%, and E = 35, while Thermomyces lanuginosus leads to c 18%, ee p 91%, and E = 26.The (S)-enantiomer was obtained by the use of Candida rugosa or Rhizopus oryzae (2-h reaction, c 34% and 35%, ee p 75 and 49%, and E = 10 and 4, respectively). Under optimal conditions, the effect of the solvent, the molar ratio, and the nucleophile were evaluated.

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Section: Methodsmentioning

confidence: 99%

“…Enantiopure alcohols, amines, and carboxylic acids are key compounds for the synthesis of many fine‐chemistry derivatives, such as pharmaceuticals, agrochemicals, and pheromones . In particular, steriochemically pure carboxylic acids are extremely useful building blocks, being easily converted into many of the other functional groups.…”

Section: Introductionmentioning

confidence: 99%

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

et al. 2017

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“…Lipase immobilization techniques have been reviewed through use of modified silicas and siliceous supports along with their applications in synthetic reactions. Recent advances in improving the enantioselectivity through medium, substrate and enzyme engineering approaches have been reviewed for free or immobilized C. antarctica lipase B . Several studies have been reported on immobilized lipases with improved performance recently, that includes the study carried out by Chen et al, in which immobilized CaL B lipases have demonstrated the desired stereoselectivity for hydrolysis of racemic 2‐O‐butyryl‐2‐phenylacetic acid under different micro environment.…”

Section: Major Challenges With Respect To Industrial Implementationmentioning

confidence: 99%

“…Recent advances in improving the enantioselectivity through medium, substrate and enzyme engineering approaches have been reviewed for free or immobilized C. antarctica lipase B. 44 Several studies have been reported on immobilized lipases with improved performance recently, that includes the study carried out by Chen et al, 291 in which immobilized CaL B lipases have demonstrated the desired stereoselectivity for hydrolysis of racemic 2-O-butyryl-2-phenylacetic acid under different micro environment. Further, from the study by Molawa et al 292 it can be noted that, bioimprinting is one of the efficient methods used for achieving improved lipases in organic media.…”

Section: Improved Lipasesmentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

297

148

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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“…Moreover, the demand for novel lipases production is intense and increasing day to day . Lipase B, from Candida antarctica (CALB), is the most important enzyme used in the industry , revealing an efficient catalyst for preparation of single isomer chiral drugs , synthesis of biodegradable polyesters and so on . Exploiting more novel CALB‐like lipases and illuminating its features will make great benefits for scientific or industrial application.…”

Section: Introductionmentioning

confidence: 99%

Structure and characterization of Aspergillus fumigatus lipase B with a unique, oversized regulatory subdomain

et al. 2019

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Fungal lipases are efficient and environment‐friendly biocatalysts for many industrially relevant processes. One of the most widely applied lipases in the manufacturing industry is Candida antarctica lipase B (CALB). Here, we report the biochemical and structural characterization of a novel CALB‐like lipase from an important human pathogen—Aspergillus fumigatus (AFLB), which has high sn‐1,3‐specificity toward triolein. AFLB crystal structure displays a CALB‐like catalytic domain and hosts a unique tightly closed ‘lid’ domain that contains a disulfide bridge, as well as an extra N‐terminal subdomain composed of residues 1–128 (including the helix α1–α5 located above the active site). To gain insight into the function of this novel lid and N‐terminal subdomain, we constructed and characterized a series of mutants in these two domains. Deleting the protruding bulk lid's residues, replacing the bulk and tight lid with a small and loose lid from CALB, or breaking the disulfide bridge increased the affinity of CALB for glyceride substrates and improved its catalytic activity, along with the loss of enzyme fold stability and thermostability. N‐terminal truncation mutants revealed that the N‐terminal peptide (residues 1–59) is a strong inhibitor of AFLB binding to lipid films. This peptide thus limits AFLB's penetration power and specific activity, revealing a unique enzyme activity regulatory mechanism. Our findings on the functional and structural properties of AFLB provide a better understanding of the functions of the CALB‐like lipases and pave the way for its future protein engineering. Database Structural data are available in the Protein Data Bank under the accession numbers http://www.rcsb.org/pdb/search/structidSearch.do?structureId=6IDY.

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Enantiopreference of Candida antarctica lipase B toward carboxylic acids: Substrate models and enantioselectivity thereof

Cited by 34 publications

References 212 publications

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

Convenient enzymatic resolution of (R,S)‐2‐methylbutyric acid catalyzed by immobilized lipases

Recent advances on sources and industrial applications of lipases

Structure and characterization of Aspergillus fumigatus lipase B with a unique, oversized regulatory subdomain

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