Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting

Mukherjee, Jaya; Gupta, Munishwar N.

doi:10.1016/j.tetlet.2015.05.101

Cited by 10 publications

(8 citation statements)

References 42 publications

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“…The activity and enantioselectivity of an enzyme in organic solvent has been shown to depend on its structural flexibility and, thus, on the preparation technique and the reaction conditions (solvent and temperature) . Numerous preparatory methods have been shown to affect the enantioselectivity and activity of SC to various extents . However, the main bottleneck for efficient application of such stabilized SC preparations is low stability in organic solvent .…”

Section: Introductionmentioning

confidence: 99%

“…methods have been shown to affect the enantioselectivity and activity of SC to various extents. [13,[23][24][25][26][27] However,t he main bottleneck for efficient application of such stabilized SC preparations is low stability in organic solvent. [28,29] Various methods (e.g.,a dditives, cross-linked enzyme aggregates (CLEA), surfactants, and immobilization) have been explored to improvei ts activity in organic solventa nd at elevated temperatures.…”

Section: Introductionmentioning

confidence: 99%

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Improved Enantioselectivity of Subtilisin Carlsberg towards Secondary Alcohols by Protein Engineering

2017

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Generally, the catalytic activity of subtilisin Carlsberg (SC) for transacylation reactions with secondary alcohols in organic solvent is low. Enzyme immobilization and protein engineering was performed to improve the enantioselectivity of SC towards secondary alcohols. Possible amino-acid residues for mutagenesis were found by combining available literature data with molecular modeling. SC variants were created by site-directed mutagenesis and were evaluated for a model transacylation reaction containing 1-phenylethanol in THF. Variants showing high E values (>100) were found. However, the conversions were still low. A second mutation was made, and both the E values and conversions were increased. Relative to that shown by the wild type, the most successful variant, G165L/M221F, showed increased conversion (up to 36 %), enantioselectivity (E values up to 400), substrate scope, and stability in THF.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Improved Enantioselectivity of Subtilisin Carlsberg towards Secondary Alcohols by Protein Engineering

2017

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“…TLL happens to be among the least expensive commercially available lipases. We have reported earlier that precipitation rather than lyophilization is a better strategy for “drying” (removal of bulk water) enzymes before these are placed in organic solvents [16] , [17] , [18] , [19] , [20] . Such precipitates have been called enzyme precipitated and rinsed with propanol (EPRP) or more generally enzyme precipitated and rinsed with organic solvents (EPROS).…”

Section: Introductionmentioning

confidence: 99%

“…In both approaches the dried enzyme has a highly rigid conformation which results in freezing the “induced conformation”. Recently, we have shown that EPROS of subtilisin prepared by precipitation with a substrate alcohol bioimprints the enzyme and increases its rate [20] . The dual bioimprinting by incorporating an ester substrate could enhance the reaction rates even further [20] .…”

Section: Introductionmentioning

confidence: 99%

“…Recently, we have shown that EPROS of subtilisin prepared by precipitation with a substrate alcohol bioimprints the enzyme and increases its rate [20] . The dual bioimprinting by incorporating an ester substrate could enhance the reaction rates even further [20] . The dual bioimprinting strategy in the present instance consists of precipitating the lipase with a substrate alcohol in the presence of a surfactant.…”

Section: Introductionmentioning

confidence: 99%

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Dual bioimprinting of Thermomyces lanuginosus lipase for synthesis of biodiesel

Mukherjee

Gupta

2016

Biotechnology Reports

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Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure

Gupta,

Uversky

2024

Protein Science

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The rationale for replacing the old binary of structure–function with the trinity of structure, disorder, and function has gained considerable ground in recent years. A continuum model based on the expanded form of the existing paradigm can now subsume importance of both conformational flexibility and intrinsic disorder in protein function. The disorder is actually critical for understanding the protein–protein interactions in many regulatory processes, formation of membrane‐less organelles, and our revised notions of specificity as amply illustrated by moonlighting proteins. While its importance in formation of amyloids and function of prions is often discussed, the roles of intrinsic disorder in infectious diseases and protein function under extreme conditions are also becoming clear. This review is an attempt to discuss how our current understanding of protein function, specificity, and evolution fit better with the continuum model. This integration of structure and disorder under a single model may bring greater clarity in our continuing quest for understanding proteins and molecular mechanisms of their functionality.

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Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting

Cited by 10 publications

References 42 publications

Improved Enantioselectivity of Subtilisin Carlsberg towards Secondary Alcohols by Protein Engineering

Improved Enantioselectivity of Subtilisin Carlsberg towards Secondary Alcohols by Protein Engineering

Dual bioimprinting of Thermomyces lanuginosus lipase for synthesis of biodiesel

Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure

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