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  1. Book: Immobilization of enzymes and cells

    Guisan, Jose M. / Bolivar, Juan M. / López-Gallego, Fernando

    methods and protocols

    (Methods in molecular biology ; 2100 ; Springer protocols)

    2020  

    Author's details edited by Jose M. Guisan, Juan M. Bolivar, Fernando López-Gallego, Javier Rocha-Martin
    Series title Methods in molecular biology ; 2100
    Springer protocols
    Collection
    Keywords Enzymes, Immobilized ; Biotechnology / methods ; Cells, Immobilized
    Language English
    Size XVI, 495 Seiten, Illustrationen, 26 cm
    Edition Fourth edition
    Publisher Humana Press
    Publishing place New York,NY
    Publishing country United States
    Document type Book
    Note Includes bibliographical references and index
    HBZ-ID HT020348408
    ISBN 978-1-0716-0214-0 ; 1-0716-0214-4
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -2100- verfügbar in Königswinter Königswinter

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  2. Book: Immobilization of enzymes and cells

    Guisán, José M.

    (Methods in molecular biology ; 1051 ; Springer protocols)

    2013  

    Author's details ed. by Jose M. Guisan
    Series title Methods in molecular biology ; 1051
    Springer protocols
    Collection
    Keywords Enzymes, Immobilized ; Cells, Immobilized ; Biotechnology / methods ; Immobilisiertes Enzym ; Immobilisierte Zelle
    Subject Immobilisierte Enzyme ; Enzym ; Enzymimmobilisierung
    Language English
    Size XI, 377 S. : Ill., graph. Darst.
    Edition 3. ed.
    Publisher Humana Press
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT017764472
    ISBN 978-1-62703-549-1 ; 9781627035507 ; 1-62703-549-4 ; 1627035508
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2013 A 2643 available for loan (reading room) Lesesaal EG

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  3. Book: Immobilization of enzymes and cells

    Guisán, José M.

    (Methods in biotechnology ; 22)

    2006  

    Author's details ed. by José M. Guisán
    Series title Methods in biotechnology ; 22
    Collection
    Keywords Enzymes, Immobilized ; Cells, Immobilized ; Biotechnology / methods ; Immobilisiertes Enzym ; Immobilisierte Zelle
    Subject Immobilisierte Enzyme ; Enzym ; Enzymimmobilisierung
    Language English
    Size XIV, 449 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Humana Press
    Publishing place Totowa, NJ
    Publishing country United States
    Document type Book
    HBZ-ID HT014692972
    ISBN 1-58829-290-8 ; 978-1-58829-290-2
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2006 A 2642 order for loan Magazin

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  4. Article ; Online: Various Strategies for the Immobilization of a Phospholipase C from

    Abdelkader, Ines / Guisán, Jose M / Sayari, Adel / Fernández-Lorente, Gloria

    Molecules (Basel, Switzerland)

    2024  Volume 29, Issue 7

    Abstract: In this study, the effect of various immobilization methods on the biochemical properties of phospholipase C (PLC) ... ...

    Abstract In this study, the effect of various immobilization methods on the biochemical properties of phospholipase C (PLC) from
    MeSH term(s) Bacillus cereus ; Sepharose ; Acetylcysteine ; Enzymes, Immobilized ; Type C Phospholipases ; Glyoxylates
    Chemical Substances glyoxyl agarose (105054-62-4) ; Sepharose (9012-36-6) ; Acetylcysteine (WYQ7N0BPYC) ; Enzymes, Immobilized ; Type C Phospholipases (EC 3.1.4.-) ; Glyoxylates
    Language English
    Publishing date 2024-03-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules29071467
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Enzymatic synthesis of mono- and disubstituted phospholipids by direct condensation of oleic acid and glycerophosphocholine with immobilized lipases and phospholipase

    Garcia-Quinto, Ernestina / Garcia-Garcia, Paz / Guisan, Jose M. / Fernandez-Lorente, Gloria

    Food chemistry. 2023 Feb. 01, v. 401

    2023  

    Abstract: Lysophospholipids which contain polyunsaturated fatty acids play a key role in food and cosmetic industries because of their bioactivity. Therefore, the formation of mono- and disubstituted phospholipids is quite interesting as they could be used for the ...

    Abstract Lysophospholipids which contain polyunsaturated fatty acids play a key role in food and cosmetic industries because of their bioactivity. Therefore, the formation of mono- and disubstituted phospholipids is quite interesting as they could be used for the formation of different natural liposomes. Using immobilized derivatives of lipases and phospholipases, the esterification of oleic acid with glycerophosphocholine (GPC) has been studied. Thus, derivatives were quite active in completely anhydrous media and in solvent-free reaction systems where the reaction takes place. CALB biocatalyst was able to successfully form oleoyl-LPC at 60 °C in the presence of 30 % butanone, where the synthesis rate was 100 times higher than in the absence of solvents at 40 °C. On the other hand, the best synthesis rate for dioleoyl-PC was achieved with immobilized Lecitase in a solvent-free process at 60 °C, an 83 % synthesis yield was achieved with an initial synthesis rate of 4.32 mg/mL × h × g.
    Keywords bioactive properties ; biocatalysts ; carboxylic ester hydrolases ; esterification ; food chemistry ; lysophospholipids ; oleic acid ; phospholipases
    Language English
    Dates of publication 2023-0201
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2022.134109
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 3634: Show issues

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  6. Article ; Online: Oriented immobilization of antibodies onto sensing platforms - A critical review.

    Gao, Shipeng / Guisán, José M / Rocha-Martin, Javier

    Analytica chimica acta

    2021  Volume 1189, Page(s) 338907

    Abstract: The immunosensor has been proven a versatile tool to detect various analytes, such as food contaminants, pathogenic bacteria, antibiotics and biomarkers related to cancer. To fabricate robust and reproducible immunosensors with high sensitivity, the ... ...

    Abstract The immunosensor has been proven a versatile tool to detect various analytes, such as food contaminants, pathogenic bacteria, antibiotics and biomarkers related to cancer. To fabricate robust and reproducible immunosensors with high sensitivity, the covalent immobilization of immunoglobulins (IgGs) in a site-specific manner contributes to better performance. Instead of the random IgG orientations result from the direct yet non-selective immobilization techniques, this review for the first time introduces the advances of stepwise yet site-selective conjugation strategies to give better biosensing efficiency. Noncovalently adsorbing IgGs is the first but decisive step to interact specifically with the Fc fragment, then following covalent conjugate can fix this uniform and antigens-favorable orientation irreversibly. In this review, we first categorized this stepwise strategy into two parts based on the different noncovalent interactions, namely adhesive layer-mediated interaction onto homofunctional support and layer-free interaction onto heterofunctional support (which displays several different functionalities on its surface that are capable to interact with IgGs). Further, the influence of ligands characteristics (synthesis strategies, spacer requirements and matrices selection) on the heterofunctional support has also been discussed. Finally, conclusions and future perspectives for the real-world application of stepwise covalent conjugation are discussed. This review provides more insights into the fabrication of high-efficiency immunosensor, and special attention has been devoted to the well-orientation of full-length IgGs onto the sensing platform.
    MeSH term(s) Antibodies ; Antibodies, Immobilized ; Biosensing Techniques ; Immunoassay ; Immunoglobulin Fc Fragments
    Chemical Substances Antibodies ; Antibodies, Immobilized ; Immunoglobulin Fc Fragments
    Language English
    Publishing date 2021-08-04
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 1483436-4
    ISSN 1873-4324 ; 0003-2670
    ISSN (online) 1873-4324
    ISSN 0003-2670
    DOI 10.1016/j.aca.2021.338907
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  7. Article ; Online: Glycosylation of polyphenolic compounds: Design of a self-sufficient biocatalyst by co-immobilization of a glycosyltransferase, a sucrose synthase and the cofactor UDP.

    Trobo-Maseda, Lara / Romero-Fernandez, María / Guisan, José M / Rocha-Martin, Javier

    International journal of biological macromolecules

    2023  Volume 250, Page(s) 126009

    Abstract: Glycosyltransferases catalyze the regioselective glycosylation of polyphenolic compounds, increasing their solubility without altering their antioxidant properties. Leloir-type glycosyltransferases require UDP-glucose as a cofactor to glycosylate a ... ...

    Abstract Glycosyltransferases catalyze the regioselective glycosylation of polyphenolic compounds, increasing their solubility without altering their antioxidant properties. Leloir-type glycosyltransferases require UDP-glucose as a cofactor to glycosylate a hydroxyl of the polyphenol, which is expensive and unstable. To simplify these processes for industrial implementation, the preparation of self-sufficient heterogeneous biocatalysts is needed. In this study, a glycosyltransferase and a sucrose synthase (as an UDP-regenerating enzyme) were co-immobilized onto porous agarose-based supports coated with polycationic polymers: polyethylenimine and polyallylamine. In addition, the UDP cofactor was strongly ionically adsorbed and co-immobilized with the enzymes, eliminating the need to add it separately. Thus, the optimal self-sufficient heterogeneous biocatalyst was able to catalyze the glycosylation of three polyphenolic compounds (piceid, phloretin and quercetin) with in situ regeneration of the UDP-glucose, allowing multiple consecutive reaction cycles without the addition of exogenous cofactor. A TTN value of 50 (theoretical maximum) was obtained in the reaction of piceid glycosylation, after 5 reaction cycles, using the self-sufficient biocatalyst based on an improved sucrose synthase variant. This result was 5-fold higher than the obtained using soluble cofactor and the co-immobilized enzymes, and much higher than those reported in the literature for similar processes.
    Language English
    Publishing date 2023-08-01
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2023.126009
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    Zs.B 2374: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Immobilization of Enzymes on Supports Activated with Glutaraldehyde: A Very Simple Immobilization Protocol.

    López-Gallego, Fernando / Guisan, Jose M / Betancor, Lorena

    Methods in molecular biology (Clifton, N.J.)

    2020  Volume 2100, Page(s) 119–127

    Abstract: In this chapter, we describe different approaches for the utilization of glutaraldehyde in protein immobilization. First, we focus on the covalent attachment of proteins to glutaraldehyde-activated matrixes. We describe conditions for the synthesis of ... ...

    Abstract In this chapter, we describe different approaches for the utilization of glutaraldehyde in protein immobilization. First, we focus on the covalent attachment of proteins to glutaraldehyde-activated matrixes. We describe conditions for the synthesis of such supports and provide an example of the immobilization and stabilization of a fructosyltransferase. We also describe how glutaraldehyde may be used for the cross-linking of protein-protein aggregates and protein adsorbed onto amino-activated matrixes. In these cases, glutaraldehyde bridges either two lysine groups from different protein molecules or a lysine from the protein structure and an amine group from the support. Examples of cross-linking are given for the immobilization of a D-amino acid oxidase on different amino-activated supports.
    MeSH term(s) Adsorption ; Cross-Linking Reagents/chemistry ; Enzyme Activation ; Enzyme Stability ; Enzymes, Immobilized/chemistry ; Glutaral/chemistry ; Proteins/chemistry
    Chemical Substances Cross-Linking Reagents ; Enzymes, Immobilized ; Proteins ; Glutaral (T3C89M417N)
    Language English
    Publishing date 2020-01-14
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0215-7_7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: New opportunities for immobilization of enzymes.

    Guisan, Jose M

    Methods in molecular biology (Clifton, N.J.)

    2013  Volume 1051, Page(s) 1–13

    Abstract: In this chapter, as a general introduction, we summarize our personal point of view on immobilization technique in order to prepare optimal and cost-effective biocatalysts. Special attention is paid to the improvement of enzyme properties via ... ...

    Abstract In this chapter, as a general introduction, we summarize our personal point of view on immobilization technique in order to prepare optimal and cost-effective biocatalysts. Special attention is paid to the improvement of enzyme properties via immobilization techniques. From the stabilization by multipoint covalent attachment to the generation of hydrophilic environments via post-immobilization techniques are here discussed. Immobilization techniques, a necessary tool to reuse enzyme, have to be simple and, if possible, may become a very powerful tool to greatly improve properties of every kind of enzymes: monomeric, multimeric, stable, labile, poorly selective, etc.
    MeSH term(s) Biocatalysis ; Bioreactors ; Cross-Linking Reagents/chemistry ; Crystallization ; Enzyme Stability ; Enzymes, Immobilized/chemistry ; Humans ; Hydrophobic and Hydrophilic Interactions ; Multiprotein Complexes/chemistry ; Protein Binding
    Chemical Substances Cross-Linking Reagents ; Enzymes, Immobilized ; Multiprotein Complexes
    Language English
    Publishing date 2013
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-62703-550-7_1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Enzymatic synthesis of mono- and disubstituted phospholipids by direct condensation of oleic acid and glycerophosphocholine with immobilized lipases and phospholipase.

    Garcia-Quinto, Ernestina / Garcia-Garcia, Paz / Guisan, Jose M / Fernandez-Lorente, Gloria

    Food chemistry

    2022  Volume 401, Page(s) 134109

    Abstract: Lysophospholipids which contain polyunsaturated fatty acids play a key role in food and cosmetic industries because of their bioactivity. Therefore, the formation of mono- and disubstituted phospholipids is quite interesting as they could be used for the ...

    Abstract Lysophospholipids which contain polyunsaturated fatty acids play a key role in food and cosmetic industries because of their bioactivity. Therefore, the formation of mono- and disubstituted phospholipids is quite interesting as they could be used for the formation of different natural liposomes. Using immobilized derivatives of lipases and phospholipases, the esterification of oleic acid with glycerophosphocholine (GPC) has been studied. Thus, derivatives were quite active in completely anhydrous media and in solvent-free reaction systems where the reaction takes place. CALB biocatalyst was able to successfully form oleoyl-LPC at 60 °C in the presence of 30 % butanone, where the synthesis rate was 100 times higher than in the absence of solvents at 40 °C. On the other hand, the best synthesis rate for dioleoyl-PC was achieved with immobilized Lecitase in a solvent-free process at 60 °C, an 83 % synthesis yield was achieved with an initial synthesis rate of 4.32 mg/mL × h × g.
    MeSH term(s) Phospholipases ; Oleic Acid ; Enzymes, Immobilized ; Liposomes ; Lipase ; Glycerylphosphorylcholine ; Solvents ; Lysophospholipids ; Butanones
    Chemical Substances Phospholipases (EC 3.1.-) ; Oleic Acid (2UMI9U37CP) ; Enzymes, Immobilized ; Liposomes ; Lipase (EC 3.1.1.3) ; Glycerylphosphorylcholine (60M22SGW66) ; Solvents ; Lysophospholipids ; Butanones
    Language English
    Publishing date 2022-09-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 243123-3
    ISSN 1873-7072 ; 0308-8146
    ISSN (online) 1873-7072
    ISSN 0308-8146
    DOI 10.1016/j.foodchem.2022.134109
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 3634: Show issues

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