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Direct recovery of intracellular lipase from cell lysate by adsorption on silica magnetic microparticles activated with Octyl groups

Direct recovery of intracellular lipase from cell lysate by adsorption on silica magnetic... New efficient protein purification methods need to be developed to overcome product loss during purification and to lower its final price. Magnetic adsorbents emerge as a potential support which can easily separate target biomolecules from crude biological medium. The hydrophobic adsorption of recombinant lipase from Bacillus thermocatenulatus (BTL-2) in novel silica magnetic microparticles (SMMp) was investigated aiming to directly recover it from cell lysate. The adsorbent surface of SMMp was modified by activation with octyl groups (25%–100%). Adsorptions on silica-octyl (non-magnetic) were also performed to understand the process better. Using centrifuged and dialyzed enzyme, under low ionic strength, the highest enzyme adsorption (92%) and desorption yields (50%) were obtained using SMMp-octyl-75% and SMMp-octyl-25%, respectively, due to simultaneous hydrophobic and ionic interaction between charged silanol groups and the enzyme. Direct enzyme adsorption from cell lysates under high ionic strength conditions led to a high yield of enzyme adsorption with 100% desorption using SMMp-octyl-25%. Therefore, the use of SMMp-octyl allows for a simple and highly efficient BTL-2 recovery by a one-step purification technique that can even be extended to other applications. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Brazilian Journal of Chemical Engineering Springer Journals

Direct recovery of intracellular lipase from cell lysate by adsorption on silica magnetic microparticles activated with Octyl groups

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Publisher
Springer Journals
Copyright
Copyright © Associação Brasileira de Engenharia Química 2021
ISSN
0104-6632
eISSN
1678-4383
DOI
10.1007/s43153-021-00190-7
Publisher site
See Article on Publisher Site

Abstract

New efficient protein purification methods need to be developed to overcome product loss during purification and to lower its final price. Magnetic adsorbents emerge as a potential support which can easily separate target biomolecules from crude biological medium. The hydrophobic adsorption of recombinant lipase from Bacillus thermocatenulatus (BTL-2) in novel silica magnetic microparticles (SMMp) was investigated aiming to directly recover it from cell lysate. The adsorbent surface of SMMp was modified by activation with octyl groups (25%–100%). Adsorptions on silica-octyl (non-magnetic) were also performed to understand the process better. Using centrifuged and dialyzed enzyme, under low ionic strength, the highest enzyme adsorption (92%) and desorption yields (50%) were obtained using SMMp-octyl-75% and SMMp-octyl-25%, respectively, due to simultaneous hydrophobic and ionic interaction between charged silanol groups and the enzyme. Direct enzyme adsorption from cell lysates under high ionic strength conditions led to a high yield of enzyme adsorption with 100% desorption using SMMp-octyl-25%. Therefore, the use of SMMp-octyl allows for a simple and highly efficient BTL-2 recovery by a one-step purification technique that can even be extended to other applications.

Journal

Brazilian Journal of Chemical EngineeringSpringer Journals

Published: Nov 28, 2021

Keywords: Lipase from Bacillus thermocatenulatus; Direct recovery; Purification; Magnetic adsorption; Cell lysate; Silica magnetic microparticles

References