Design of a core–shell support to improve lipase features by immobilization. Issue 67 (30th June 2016)
- Record Type:
- Journal Article
- Title:
- Design of a core–shell support to improve lipase features by immobilization. Issue 67 (30th June 2016)
- Main Title:
- Design of a core–shell support to improve lipase features by immobilization
- Authors:
- Manoel, Evelin A.
Pinto, Martina
dos Santos, José C. S.
Tacias-Pascacio, Veymar G.
Freire, Denise M. G.
Pinto, José Carlos
Fernandez-Lafuente, Roberto - Abstract:
- Abstract : Different core–shell polymeric supports, exhbiting different featured, were produced and utilized in the immobilization and tuning of different lipases. Abstract : Different core–shell polymeric supports, exhibiting different morphologies and composition, were produced through simultaneous suspension and emulsion polymerization, using styrene (S) and divinylbenzene (DVB) as co-monomers. Supports composed of polystyrene in both the core and the shell (PS/PS) and the new poly(styrene- co -divinylbenzene) support (PS- co -DVB/PS- co -DVB) were used for the immobilization of three different lipases (from Rhizomucor miehie (RML), from Themomyces lanuginosus (TLL) and the form B from Candida antarctica, (CALB)) and of the phospholipase Lecitase Ultra (LU). The features of the new biocatalysts were evaluated and compared to the properties of commercial biocatalysts (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM) and biocatalysts prepared by enzyme immobilization onto commercial octyl-agarose, a support reported as very suitable for lipase immobilization. It was shown that protein loading and stability of the biocatalysts prepared with the core–shell supports were higher than the ones obtained with commercial octyl-agarose or the commercial lipase preparations. Besides, it was shown that the biocatalysts prepared with the core–shell supports also presented higher activities than commercial biocatalysts when employing different substrates, encouraging the use ofAbstract : Different core–shell polymeric supports, exhbiting different featured, were produced and utilized in the immobilization and tuning of different lipases. Abstract : Different core–shell polymeric supports, exhibiting different morphologies and composition, were produced through simultaneous suspension and emulsion polymerization, using styrene (S) and divinylbenzene (DVB) as co-monomers. Supports composed of polystyrene in both the core and the shell (PS/PS) and the new poly(styrene- co -divinylbenzene) support (PS- co -DVB/PS- co -DVB) were used for the immobilization of three different lipases (from Rhizomucor miehie (RML), from Themomyces lanuginosus (TLL) and the form B from Candida antarctica, (CALB)) and of the phospholipase Lecitase Ultra (LU). The features of the new biocatalysts were evaluated and compared to the properties of commercial biocatalysts (Novozym 435 (CALB), Lipozyme RM IM and Lipozyme TL IM) and biocatalysts prepared by enzyme immobilization onto commercial octyl-agarose, a support reported as very suitable for lipase immobilization. It was shown that protein loading and stability of the biocatalysts prepared with the core–shell supports were higher than the ones obtained with commercial octyl-agarose or the commercial lipase preparations. Besides, it was shown that the biocatalysts prepared with the core–shell supports also presented higher activities than commercial biocatalysts when employing different substrates, encouraging the use of the produced core–shell supports for immobilization of lipases and the development of new applications. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 67(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 67(2016)
- Issue Display:
- Volume 6, Issue 67 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 67
- Issue Sort Value:
- 2016-0006-0067-0000
- Page Start:
- 62814
- Page End:
- 62824
- Publication Date:
- 2016-06-30
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c6ra13350a ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2905.xml