Biocatalytic Applications

Faber, Kurt

doi:10.1007/978-3-319-61590-5_2

Cited by 12 publications

(6 citation statements)

References 1,678 publications

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“…In the case of a reaction with rac-2-O-Butyryl-2-phenylacetic acid (precursor of mandelic acid derivatives APIs as pemoline ([ 150 ], Scheme 7 ), homatropine, cyclandelate, cephalosporin, antineoplastics, antiobesity and anti-thrombotic agents [ 150 , 151 , 152 ]), BTL2 immobilized in octyl-agarose, butyl-agarose, butyl-Toyopearl ® or hexyl-Toyopearl ® , showed preference for enantiomer (S), with values of the enantiomeric ratio (E) from 8 to >100, the latter for the octyl-agarose derivative [ 149 ] ( Table 2 ). These observed increases by changing the support in E values are key for applications because, as a rule of thumb, values below fifteen are considered insufficient; from 15–30 moderate to good, and above this, excellent [ 153 ]. CAL B, TLL and Lecitase ® demonstrated less marked changes when immobilized in such supports; for example, the derivatives of CAL B changed their values of E from 3 to 60 for the derivative butyl-Toyopearl ® and octyl-agarose, respectively [ 149 ] ( Table 2 ).…”

Section: Immobilization Of Lipasesmentioning

confidence: 99%

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks

Godoy

Pardo‐Tamayo

Barbosa

2022

IJMS

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Processes involving lipases in obtaining active pharmaceutical ingredients (APIs) are crucial to increase the sustainability of the industry. Despite their lower production cost, microbial lipases are striking for their versatile catalyzing reactions beyond their physiological role. In the context of taking advantage of microbial lipases in reactions for the synthesis of API building blocks, this review focuses on: (i) the structural origins of the catalytic properties of microbial lipases, including the results of techniques such as single particle monitoring (SPT) and the description of its selectivity beyond the Kazlauskas rule as the “Mirror-Image Packing” or the “Key Region(s) rule influencing enantioselectivity” (KRIE); (ii) immobilization methods given the conferred operative advantages in industrial applications and their modulating capacity of lipase properties; and (iii) a comprehensive description of microbial lipases use as a conventional or promiscuous catalyst in key reactions in the organic synthesis (Knoevenagel condensation, Morita–Baylis–Hillman (MBH) reactions, Markovnikov additions, Baeyer–Villiger oxidation, racemization, among others). Finally, this review will also focus on a research perspective necessary to increase microbial lipases application development towards a greener industry.

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Section: Immobilization Of Lipasesmentioning

confidence: 99%

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks

Godoy

Pardo‐Tamayo

Barbosa

2022

IJMS

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“…The questionable atom economy and also efficiency of such systems has triggered an interest in utilizing enzymes as biocatalysts for such transformations. Enzymes from several different classes are able to catalyze the two‐electron transfer from an alcohol to an acceptor and may therefore serve as candidate biocatalysts . The enzyme superfamily of alcohol dehydrogenases (ADHs) contains enzymes dependent on NAD(P) + or NAD(P)H, as an acceptor and donor, respectively, for hydride transfer reactions between alcohols and the cognate carbonyl compounds.…”

Section: Introductionmentioning

confidence: 99%

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer

et al. 2017

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Alcohol dehydrogenase A (ADH-A) from Rhodococcus ruber DSM 44541 is a promising biocatalyst for redox transformations of arylsubstituted sec-alcohols and ketones. The enzyme is stereoselective in the oxidation of 1-phenylethanol with a 300-fold preference for the (S)-enantiomer. The low catalytic efficiency with (R)-1-phenylethanol has been attributed to nonproductive binding of this substrate at the active site. Aiming to modify the enantioselectivity, to rather favor the (R)-alcohol, and also test the possible involvement of nonproductive substrate binding as a mechanism in substrate discrimination, we performed directed laboratory evolution of ADH-A. Three targeted sites that contribute to the active-site cavity were exposed to saturation mutagenesis in a stepwise manner and the generated variants were selected for improved catalytic activity with (R)-1-phenylethanol. After three subsequent rounds of mutagenesis, selection and structure-function analysis of isolated ADH-A variants, we conclude: (1) W295 has a key role as a structural determinant in the discrimination between (R)-and (S)-1-phenylethanol and a W295A substitution fundamentally changes the stereoselectivity of the protein. One observable effect is a faster rate of NADH release, which changes the rate-limiting step of the catalytic cycle from coenzyme release to hydride transfer. (2) The obtained change in enantiopreference, from the (S)-to the (R)-alcohol, can be partly explained by a shift in the nonproductive substrate binding modes.

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“…The mechanism of action involves a nucleophilic group of a residue in the active site (e.g., the carboxylate group of an aspartic acid in pepsin, the hydroxy group of a serine in serine hydrolases or the thiol of a cysteine in papain) that attacks the corresponding electrophilic substrate to form a covalent acyl–enzyme intermediate [ 51 , 52 , 53 ]. Then, water or any other nucleophile that can compete with the water (e.g., when working in organic solvents at low water concentration), attacks the acyl–enzyme intermediate, regenerating the enzyme, affording the final product [ 54 ]. In recent years, DESs have received more attention in the field of saccharification than in terms of the organic synthesis of molecules.…”

Section: Hydrolysismentioning

confidence: 99%

Combination of Enzymes and Deep Eutectic Solvents as Powerful Toolbox for Organic Synthesis

et al. 2023

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During the last decade, a wide spectrum of applications and advantages in the use of deep eutectic solvents for promoting organic reactions has been well established among the scientific community. Among these synthetic methodologies, in recent years, various examples of biocatalyzed processes have been reported, making use of eutectic mixtures as reaction media, as an improvement in terms of selectivity and sustainability. This review aims to show the newly reported protocols in the field, subdivided by reaction class as a ‘toolbox’ guide for organic synthesis.

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Biocatalytic Applications

Cited by 12 publications

References 1,678 publications

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks

Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer

Combination of Enzymes and Deep Eutectic Solvents as Powerful Toolbox for Organic Synthesis

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