Chemical amination of immobilized enzymes for enzyme coimmobilization: Reuse of the most stable immobilized and modified enzyme

Lipase from Yarrowia lipolytica: Prospects as an Industrial Biocatalyst for Biotechnological Applications

“…In summary, using heterofunctional supports in enzymatic immobilization is essential because it allows greater efficiency and specificity in enzyme fixation [249][250][251], which results in more excellent stability and reuse capability, in addition to allowing the creation of multifunctional systems [252]. These systems lead to the performance of several consecutive reactions based on the possibility of immobilizing several different enzymes on the same support [253].…”

Reutilization of the Most Stable Coimmobilized Enzyme Using Glutaraldehyde Chemistry to Produce a New Combi-biocatalyst When the Coimmobilized Enzyme with a Lower Stability Is Inactivated

“…Now, we want to focus on a specific problem: the coimmobilization of two enzymes that, after immobilization, exhibit very different stabilities; e.g., one is almost fully inactivated after some reaction cycles, while the other immobilized enzyme remains almost fully active. , Using conventional coimmobilization protocols, all the enzymes that are coimmobilized must be cast off, although some of them remain in full activity. , Some strategies have been recently launched to overcome this matter. − All are founded on the coimmobilization of the diverse enzymes utilizing diverse immobilization strategies in such a way that the least stable coimmobilized enzyme may be eliminated from the biocatalysts without affecting the stable and almost fully active coimmobilized enzyme(s). Some strategies modify the previously immobilized most stable enzyme to convert it into an ion exchanger. ,, Other strategies modify the support used for previous covalent immobilization of the most stable immobilized enzyme to transform it into an anion exchanger. , Other strategies use heterofunctional supports. , The latter is similar to the proposal we present in this research effort. Here, we launch the use of aminated supports to coimmobilize enzymes using glutaraldehyde chemistry. − Glutaraldehyde is a quite adaptable immobilization reagent.…”

“…Some strategies modify the previously immobilized most stable enzyme to convert it into an ion exchanger. 30,31,33 Other strategies modify the support used for previous covalent immobilization of the most stable immobilized enzyme to transform it into an anion exchanger. 32,34 Other strategies use heterofunctional supports.…”

Multienzymatic Catalysis and Enzyme Co-Immobilization

“…This way, new strategies where the most stable enzymes are immobilized following a strategy that is different to the one used for the least stable enzymes (which must be immobilized via a reversible immobilization technique) have been developed [35]. Thus, the most stable co-immobilized enzymes may be converted into ionic exchangers via physical or chemical modification, and the least stable enzymes may be then immobilized over them [38]. After their inactivation, the least stable enzymes may be released to the medium and the biocatalyst reused to build a new combibiocatalyst.…”