Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate
In this study, the modulation of enzymatic biocatalysts were developed by the use of lipase B from Candida antarctica covalently immobilized on an eco-friendly support, cashew apple bagasse, activated with 10% glycidol–ethylenediamine–glutaraldehyde (GEG) under different immobilization strategies (5...
Saved in:
Published in | Bioprocess and biosystems engineering Vol. 43; no. 12; pp. 2253 - 2268 |
---|---|
Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Springer Berlin Heidelberg
01.12.2020
Springer Nature B.V |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | In this study, the modulation of enzymatic biocatalysts were developed by the use of lipase B from
Candida antarctica
covalently immobilized on an eco-friendly support, cashew apple bagasse, activated with 10% glycidol–ethylenediamine–glutaraldehyde (GEG) under different immobilization strategies (5 mM or 100 mM ionic strength and in absence or presence of 0.5% (v/v) Triton X-100). The biocatalysts were characterized for thermal and organic solvents stabilities and compared with the soluble enzyme. The biocatalysts were then applied to the hydrolysis of the
rac
-indanyl acetate (2:1 ratio enzyme/substrate) at pH 7.0 and 30 °C for 24 h. For all the strategies evaluated, GEG promoted kinetic resolution of
rac
-indanyl acetate with maximum conversion (50%) and led to (
R
)-indanol with excellent enantiomeric excess (97%), maintaining the maximum conversion for five consecutive cycles of hydrolysis. Therefore, the use of cashew apple bagasse has proved to be a promising eco-friendly support for enzyme immobilization, since it resulted in stable biocatalysts for enzymatic kinetic resolution.
Graphic abstract |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1615-7591 1615-7605 |
DOI: | 10.1007/s00449-020-02411-8 |