Esterases as stereoselective biocatalysts

Romano, Diego; Bonomi, Francesco; Mattos, Marcos Carlos de; Fonseca, Thiago de Sousa; Oliveira, Maria da Conceição Ferreira de; Molinari, Francesco

doi:10.1016/j.biotechadv.2015.01.006

Cited by 77 publications

(45 citation statements)

References 121 publications

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“…Such an overall phenomenon is generally referred to as "interfacial activation" [35]. Due to their advantageous biochemical properties, such as high chemo, regio and stereoselectivity, and thermostability, microbial carboxylesterases find numerous industrial applications in a wide range of sectors [4][5][6]. Kinetic resolution of racemic esters of chiral alcohols via their enantioselective hydrolysis is among the most studied application.…”

Section: Discussionmentioning

confidence: 99%

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

et al. 2018

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Section: Discussionmentioning

confidence: 99%

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

et al. 2018

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“…Promiscuous esterases acting against multiple substrates, while at the same time being enantio-selective, appear to be rare in nature, or at least in the habitats from where the esterases herein described were isolated [5]. As these enzymes are of interest for application purposes [1][2][3][4][5][6]32], protein engineering and rational design may be needed to obtain esterases being promiscuous and selective for industrial applications. We anticipate that the possibility to transform a promiscuous but not selective esterase into an efficient enantio-selective biocatalyst would require less engineering effort because increasing the selectivity for an enantiomer may involve a reduced number of contacts close to the active sites (for a recent example see reference [33]).…”

Section: Discussionmentioning

confidence: 99%

Relationships between Substrate Promiscuity and Chiral Selectivity of Esterases from Phylogenetically and Environmentally Diverse Microorganisms

et al. 2018

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Substrate specificity and selectivity of a biocatalyst are determined by the protein sequence and structure of its active site. Finding versatile biocatalysts acting against multiple substrates while at the same time being chiral selective is of interest for the pharmaceutical and chemical industry. However, the relationships between these two properties in natural microbial enzymes remain underexplored. Here, we performed an experimental analysis of substrate promiscuity and chiral selectivity in a set of 145 purified esterases from phylogenetically and environmentally diverse microorganisms, which were assayed against 96 diverse esters, 20 of which were enantiomers. Our results revealed a negative correlation between substrate promiscuity and chiral selectivity in the evaluated enzymes. Esterases displaying prominent substrate promiscuity and large catalytic environments are characterized by low chiral selectivity, a feature that has limited commercial value. Although a low level of substrate promiscuity does not guarantee high chiral selectivity, the probability that esterases with smaller active sites possess chiral selectivity factors of interest for industry (>25) is significantly higher than for promiscuous enzymes. Together, the present study unambiguously demonstrates that promiscuous and selective esterases appear to be rare in nature and that substrate promiscuity can be used as an indicator of the chiral selectivity level of esterases, and vice versa.

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“…4H). This is likely to be attributed to the hydrolytic [78] or non-specific enzymatic degradation [79] of ester bonds formed by the methacrylation of alginate hydroxyl groups [40]. However, dynamic shear loading partially reversed the decrease in construct stiffness, resulting in higher compressive moduli of shear stimulated ALMA and PEG-80S constructs when compared to static controls cultured for the same period of time (Fig.…”

Section: Discussionmentioning

confidence: 99%

Tailoring hydrogel surface properties to modulate cellular response to shear loading

et al. 2017

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Biological tissues at articulating surfaces, such as articular cartilage, typically have remarkable low-friction properties that limit tissue shear during movement. However, these frictional properties change with trauma, aging, and disease, resulting in an altered mechanical state within the tissues. Yet, it remains unclear how these surface changes affect the behaviour of embedded cells when the tissue is mechanically loaded. Here, we developed a cytocompatible, bilayered hydrogel system that permits control of surface frictional properties without affecting other bulk physicochemical characteristics such as compressive modulus, mass swelling ratio, and water content. This hydrogel system was applied to investigate the effect of variations in surface friction on the biological response of human articular chondrocytes to shear loading. Shear strain in these hydrogels during dynamic shear loading was significantly higher in high-friction hydrogels than in low-friction hydrogels. Chondrogenesis was promoted following dynamic shear stimulation in chondrocyte-encapsulated low-friction hydrogel constructs, whereas matrix synthesis was impaired in high-friction constructs, which instead exhibited increased catabolism. Our findings demonstrate that the surface friction of tissue-engineered cartilage may act as a potent regulator of cellular homeostasis by governing the magnitude of shear deformation during mechanical loading, suggesting a similar relationship may also exist for native articular cartilage.

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Esterases as stereoselective biocatalysts

Cited by 77 publications

References 121 publications

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

A stereospecific carboxyl esterase from Bacillus coagulans hosting nonlipase activity within a lipase‐like fold

Relationships between Substrate Promiscuity and Chiral Selectivity of Esterases from Phylogenetically and Environmentally Diverse Microorganisms

Tailoring hydrogel surface properties to modulate cellular response to shear loading

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