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Green Chemistry
Page 10 of 11
DOI: 10.1039/C7GC00896A
ARTICLE
Green Chemistry
open-lid and closed-lid conformations of lipase B from of
Candida antarctica enabled efficient selection of organosilanes
serving as components of ternary compositions to prepare sol-
gel matrices for entrapment of CaLB, an enzyme widely
applied in various industrial processes.
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Immobilization engineering was further aided by response
surface methodology leading to novel ways of CaLB
immobilization with enhanced functional efficiency and
reusability.
The novel biocatalysts were prepared by entrapment of CaLB
in sol-gel matrices using three different ternary compositions
of organosilanes. The systems were tested in kinetic resolution
of two racemic alcohols and two racemic amines. Rational
selection of the organosilane precursors enabled the
preparation of highly efficient and enantioselective
biocatalysts. We also found that there exists no single “best”
silane precursor composition and each substrate requires
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individual optimization. Therefore, our approach,
a
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combination of computational and experimental methods
which can highly accelerate the optimization process, is of
general importance and can significantly contribute to the
dissemination of an inherently green methodology.
In kinetic resolutions of secondary alcohols and secondary
amines substituted with aromatic or aliphatic substituents, sol-
gel-entrapped CaLBs were superior to the traditional polymer-
based forms. They are characterized by enhanced thermal
stability in organic media, improved recyclability and higher
operational stability both in batch and continuous mode
operations.
The space-time yield in the range of 0.81 – 1.21 kg L-1 h-1 and
the specific productivity in the range of 0.44 – 0.66 kg g-1 day-1
observed with the various sol-gel entrapped forms of CaLB in
continuous-mode KRs of selected alcohol and amine
substrates as well as facile up scaling of the immobilization
process (up to 100-fold from lab scale) and a potential to
produce more than 2.5 kg product/g native enzyme render our
method as a tunable and economic green option to produce
biocatalysts for flow chemistry.
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Acknowledgements
Financial support from the New Hungary Development Plan
(TÁMOP-4.2.1/B-09/1/KMR-2010-0002) is acknowledged.
Licensing of the Schrödinger Suite software package was
financed by the Hungarian OTKA Foundation (K 108793). WD
thanks the UNKP-PD-416 program for financial support. We
thank Prof. Mihály Nógrádi (BME, Budapest) for helpful
discussions.
References and notes
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10 | Green Chemistry., 2017, 00, 1-10
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