Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

• Published in: Biotechnology advances Vol. 37; no. 5; pp. 746 - 770
• Main Authors: Rodrigues, Rafael C., Virgen-Ortíz, Jose J., dos Santos, José C.S., Berenguer-Murcia, Ángel, Alcantara, Andres R., Barbosa, Oveimar, Ortiz, Claudia, Fernandez-Lafuente, Roberto
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.09.2019; Elsevier Science Ltd
• Subjects: Acyl-vinylsulfone supports; amination; biocatalysis; biocatalysts; Biotechnology - methods; Coimmobilization; Cross-Linking Reagents - chemistry; Crosslinking; Deactivation; Desorption; detergents; Enzyme amination; Enzyme coimmobilization; Enzyme Stability; Enzymes; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; epoxides; Glutaral - chemistry; Glutaraldehyde; Heterofunctional supports; High temperature; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Immobilization; immobilized enzymes; Intermolecular lipase crosslinking; ionic strength; Lipase; Lipase - chemistry; Lipase - metabolism; Lipase immobilization; Lipase interfacial activation; moieties; Organic chemistry; Solvents - chemistry; temperature; triacylglycerol lipase; Acyl-vinylsulfone supports; Enzyme coimmobilization; Heterofunctional supports; Lipase interfacial activation; Intermolecular lipase crosslinking; Enzyme amination; Lipase immobilization

Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main caus...