Enhancing the resolution of (R,S)-2-octanol catalyzed by magnetic cross-linked lipase aggregates using an alternating magnetic field

Liu, Ying; Chen, Guo; Liu, Chun-Zhao

doi:10.1016/j.cej.2015.05.089

Cited by 26 publications

(15 citation statements)

References 29 publications

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“…The movement of magnetic immobilized laccase with constantly changed direction under alternating magnetic field has better stirring function than the movement with constant direction under mechanical stirring. The results were well in agreement with those observed by Liu and Zheng . They, respectively, obtained enhanced resolution of (R,S)‐2‐octanol and intensified bi‐enzyme reactions with application of an alternating magnetic field.…”

Section: Resultsmentioning

confidence: 97%

“…However, vigorous agitation is likely to damage the immobilized enzyme and is not usable in micro‐reactors . Magnetic fields have been applied in many reactions catalyzed by magnetic carrier supported enzyme to improve the stirring method . Magnetic carriers oscillate and behave like microscopic stirrers to facilitate mass transfer processes in the reaction.…”

Section: Introductionmentioning

confidence: 99%

“…Liu et al . reported that the resolution of ( R,S )‐2‐octanol catalyzed by magnetic crosslinked lipase aggregates using an alternating magnetic field was also improved . The motions of the magnetic carriers under an alternating magnetic field are realized by trying to align in the direction of the continuously changing magnetic field …”

Section: Introductionmentioning

confidence: 99%

“…12 Magnetic fields have been applied in many reactions catalyzed by magnetic carrier supported enzyme to improve the stirring method. [13][14][15] Magnetic carriers oscillate and behave like microscopic stirrers to facilitate mass transfer processes in the reaction. For instance, the group of Sakai et al found that enzyme reaction of magnetically anisotropic polyacrylamide gel rods immobilized with ferromagnetic powder and ß-D-galactosidase were enhanced in an alternating magnetic field.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Xia

Wan

Liu

et al. 2017

J of Chemical Tech & Biotech

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Xia

Wan

Liu

et al. 2017

J of Chemical Tech & Biotech

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“…Therefore, the high purity of β‐CD obtained at 50 °C shows that CGTase processed through CLEA technology at high temperature (85 °C) can form and maintain the conformation with better specificity. This method is an additional approach to enhance product specificity besides using chemicals addition and alternating magnetic field . In this study, the total conversion proportion of potato starch was relative low because the residual activity of CGTase was low and the barrier to potato starch permeating as potato starch was macromolecular.…”

Section: Resultsmentioning

confidence: 93%

Cross‐linked enzyme aggregates of recombinant cyclodextrin glycosyltransferase for high‐purity β‐cyclodextrin production

Zhang

Mao

2019

J of Chemical Tech & Biotech

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BACKGROUND High‐purity α‐, β‐, or γ‐cyclodextrin (CD) production using cyclodextrin glycosyltransferase (CGTase) as biocatalyst to cyclize starch is advantageous owing to its low cost of purification and product specificity. Several approaches have been investigated to enhance product specificity of CGTase, such as new CGTase isolation, CGTase gene (cgt) mutation, and chemical addition. RESULTS Recombinant CGTase was cross‐linked by glutaraldehyde to obtain cross‐linked enzyme aggregates of recombinant CGTase (CLEA‐CGTase) at 85 °C because free CGTase showed high product specificity at 85 °C. The CLEA‐CGTase was prepared under the conditions 75 U mL−1 CGTase with 0.1% (v/v) glutaraldehyde for 10 min at 85 °C after optimization first, and produced a high proportion of β‐CD from soluble starch at 50 °C in the conversion system. The conversion process was carried out with 10 to 200 U mL−1 CLEA‐CGTase, resulting in 100% β‐CD from soluble starch after 420 min conversion of the potato starch solution at 50 °C. And the proportion of β‐CD was still higher than 90% when 8000 U mL−1 CLEA‐CGTase was added. CONCLUSIONS CLEA technology maintained CGTase conformation of 85 °C, and produced a high proportion of β‐CD at 50 °C. This research showed the CLEA technology kept the conformation of enzyme for specific product production. © 2018 Society of Chemical Industry

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Pilot‐scale development of core–shell polymer supports for the immobilization of recombinant lipase B from Candida antarctica and their application in the production of ethyl esters from residual fatty acids

Cipolatti

Pinto

Robert

et al. 2018

J of Applied Polymer Sci

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A recombinant lipase B from Candida antarctica (LipB) in Pichia pastoris was synthesized through submerged fermentation using crude glycerin as substrate. The immobilization of this enzyme on the core–shell polymeric supports is an effective alternative for its application. The supports with distinct levels of hydrophobicity were produced through combined suspension and emulsion polymerization in pilot scale. Particles with distinct compositions were synthesized (PMMA/PMMA; PMMA‐co‐DVB/PMMA‐co‐DVB; and PS‐co‐DVB/PS‐co‐DVB) and employed on the immobilization of the produced lipase (LipB) and the commercial enzyme (CalB). The morphological properties (specific area, average pore diameter, specific volume of pores, and hydrophobicity level) and the influence of the polymerization conditions on the morphology of the supports were studied. The thermal stability of such biocatalysts was also investigated in the presence of calcium cation (Ca+2), maintained 100% of the activity after 3 h at 50°C when the PMMA‐co‐DVB/PMMA‐co‐DVB was employed. The synthesized enzyme and supports manufactured in pilot scale were employed successfully for production of esters using residual fatty acids as substrates, adding value to these raw materials and increasing the ranges of possible applications.

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Enhancing the resolution of (R,S)-2-octanol catalyzed by magnetic cross-linked lipase aggregates using an alternating magnetic field

Cited by 26 publications

References 29 publications

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Cross‐linked enzyme aggregates of recombinant cyclodextrin glycosyltransferase for high‐purity β‐cyclodextrin production

Pilot‐scale development of core–shell polymer supports for the immobilization of recombinant lipase B from Candida antarctica and their application in the production of ethyl esters from residual fatty acids

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