Next Article in Journal
Preparative Separation and Purification of the Total Flavonoids in Scorzonera austriaca with Macroporous Resins
Next Article in Special Issue
Construction of an Immobilized Thermophilic Esterase on Epoxy Support for Poly(ε-caprolactone) Synthesis
Previous Article in Journal
Antifungal Activity and Biochemical Response of Cuminic Acid against Phytophthora capsici Leonian
Previous Article in Special Issue
Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)
Article Menu
Issue 6 (June) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(6), 767; doi:10.3390/molecules21060767

Tailoring the Spacer Arm for Covalent Immobilization of Candida antarctica Lipase B—Thermal Stabilization by Bisepoxide-Activated Aminoalkyl Resins in Continuous-Flow Reactors

1
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest H-1111, Hungary
2
SynBiocat LLC; Lövőház u. 19/1, Budapest H-1043, Hungary
*
Author to whom correspondence should be addressed.
Academic Editor: Roberto Fernandez-Lafuente
Received: 10 May 2016 / Revised: 7 June 2016 / Accepted: 8 June 2016 / Published: 13 June 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
View Full-Text   |   Download PDF [3148 KB, uploaded 13 June 2016]   |  

Abstract

An efficient and easy-to-perform method was developed for immobilization of CaLB on mesoporous aminoalkyl polymer supports by bisepoxide activation. Polyacrylate resins (100–300 µm; ~50 nm pores) with different aminoalkyl functional groups (ethylamine: EA and hexylamine: HA) were modified with bisepoxides differing in the length, rigidity and hydrophobicity of the units linking the two epoxy functions. After immobilization, the different CaLB preparations were evaluated using the lipase-catalyzed kinetic resolution (KR) of racemic 1-phenylethanol (rac-1) in batch mode and in a continuous-flow reactor as well. Catalytic activity, enantiomer selectivity, recyclability, and the mechanical and long-term stability of CaLB immobilized on the various supports were tested. The most active CaLB preparation (on HA-resin activated with 1,6-hexanediol diglycidyl ether—HDGE) retained 90% of its initial activity after 13 consecutive reaction cycles or after 12 month of storage at 4 °C. The specific rate (rflow), enantiomer selectivity (E) and enantiomeric excess (ee) achievable with the best immobilized CaLB preparations were studied as a function of temperature in kinetic resolution of rac-1 performed in continuous-flow packed-bed bioreactors. The optimum temperature of the most active HA-HDGE CaLB in continuous-flow mode was 60 °C. Although CaLB immobilized on the glycerol diglycidyl ether (GDGE)-activated EA-resin was less active and less selective, a much higher optimum temperature (80 °C) was observed with this form in continuous-flow mode KR of rac-1. View Full-Text
Keywords: lipase; immobilization; covalent attachment; kinetic resolution; thermal stabilization; continuous-flow reactor lipase; immobilization; covalent attachment; kinetic resolution; thermal stabilization; continuous-flow reactor
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Abaházi, E.; Lestál, D.; Boros, Z.; Poppe, L. Tailoring the Spacer Arm for Covalent Immobilization of Candida antarctica Lipase B—Thermal Stabilization by Bisepoxide-Activated Aminoalkyl Resins in Continuous-Flow Reactors. Molecules 2016, 21, 767.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top