Modulation of lipase B from Candida antarctica properties via covalent immobilization on eco-friendly support for enzymatic kinetic resolution of rac-indanyl acetate.

Abstract:

: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.

journal_name

Bioprocess Biosyst Eng

authors

de Souza TC,de Sousa Fonseca T,de Sousa Silva J,Lima PJM,Neto CACG,Monteiro RRC,Rocha MVP,de Mattos MC,Dos Santos JCS,Gonçalves LRB

doi

10.1007/s00449-020-02411-8

subject

Has Abstract

pub_date

2020-12-01 00:00:00

pages

2253-2268

issue

12

eissn

1615-7591

issn

1615-7605

pii

10.1007/s00449-020-02411-8

journal_volume

43

pub_type

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