Thermal and Mechanical Stability of Immobilized Candida antarctica Lipase B: an Approximation to Mechanochemical Energetics in Enzyme Catalysis

Very recently, several successful enzymatic processes performed with mechanical activation have been disclosed; that is, despite the mechanical stress caused by High‐Speed Ball‐Milling, immobilized enzymes can retain activity. In the present study, the effect of thermal and mechanical stress was exa...

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Bibliographic Details
Published in:ChemCatChem 2020-02, Vol.12 (3), p.803-811
Main Authors: Pérez‐Venegas, Mario, Tellez‐Cruz, Miriam M., Solorza‐Feria, Omar, López‐Munguía, Agustín, Castillo, Edmundo, Juaristi, Eusebio
Format: Article
Language:English
Subjects:
Biocatalyst
Biotransformation
CALB
Catalysis
Deactivation
Denaturation
Enzymes
Lipase
Mechanoenzymatic
Mechanostability
Stability
Sustainable
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Summary:Very recently, several successful enzymatic processes performed with mechanical activation have been disclosed; that is, despite the mechanical stress caused by High‐Speed Ball‐Milling, immobilized enzymes can retain activity. In the present study, the effect of thermal and mechanical stress was examined as potential inducers of enzymatic denaturation, when using either free, immobilized, or ground immobilized enzyme. The recorded observations show a remarkable stability of ground immobilized enzyme. Moreover, ground biocatalyst turns out to exhibit an increase of one order of magnitude in the efficiency of the catalytic process, maintaining excellent enantiodiscrimination, without significant activity loss even after four milling cycles. These observations rule out enzyme inactivation as direct consequence of the milling process. Additionally, boosted enzyme efficiency was used to optimize a relatively inefficient chiral amine resolution reaction, achieving a 25 % faster biotransformation (in 45 min) and yielding essentially enantiopure products (ee>99%, E>500). Beating enzymes for breakfast: For the first time, the effect of grinding over enzyme activity and stability was systematically studied. The results indicate a high enzyme stability to the mechanochemical conditions and, unexpectedly, and increment in enzyme activity of one order of magnitude after the mechanochemical process without loss in enantiopreference of the enzyme.
ISSN:1867-3880
1867-3899
DOI:10.1002/cctc.201901714