New monolithic enzymatic micro-reactor for the fast production and purification of oligogalacturonides

Monolithic bioreactors: Effect of chymotrypsin immobilization on its biocatalytic properties

“…However, there are a significant amount of reports on application of GMA-EDMA monolithic materials for the preparation of flowthrough bioreactors based on different enzymes, e.g. immobilized invertase [24], polynucleotide phosphorylase [25], glucose oxidase [26], citrate lyase, malate dehydrogenase, isocitrate dehydrogenase, lactate dehydrogenase [27], papain [28], lignin peroxidase [29], deoxyribonuclease [30,31], elastase [32], chymotrypsin [33], beta-secretase [34], pronase [35], pectin lyase [36] glucuronan lyase [37], pepsin [38] and peptide-N-glycosidase F [39].…”

Synthesis of a monolithic, micro-immobilised enzyme reactor via click-chemistry

“…Different micro-IMERs carrying CT, acetylcholinesterase, β-secretase or pectin lyase were fabricated using CIM disc as solid matrix [10,20,28]. All these IMERs were operated with the mobile phase flow rates in the range of 0.2-1.5 mL/min and by injecting sample substrate solutions with volumes ranging between 10 and 50 μL.…”

“…The papers describing reactors obtained via immobilisation of trypsin on glycidyl methacrylate-ethylene dimethacrylate (GMA-EDMA) or silica monoliths and intended for protein digestion were presented in the current literature [2][3][4][5][6][7]. However, there are a considerable number of reports on implementation of monolithic materials for the preparation of flow-through reactors on the basis of different enzymes such as elastase [8] polynucleotide phosphorylase [9], betasecretase [10], citrate lyase, malate dehydrogenase, isocitrate dehydrogenase, lactate dehydrogenase [11], papain [12], lignin peroxidase [13], deoxyribonuclease [14,15], trypsin [16], chymotrypsin [17], invertase [18], pronase [19], pectin lyase [20] and glucose oxidase [21].…”

Biotechnological potential of pectinolytic complexes of fungi

“…Immobilization also allows recovery and reuses of enzymes, avoiding its presence in the final product, the ability to use multi-enzyme reactions, artificial metabolic pathways and the compartmentalization of catalytic reactions (Brady and Jordaan 2009). For immobilization of pectinases, several methods have been developed using different supports such as nylon (Vaillant et al 2000;Diano et al 2008), Eupergit C (Spagna et al 1995), glass (Diano et al 2008), chitosan and chitin (Vaillant et al 2000), polyacrylonitrile (Diano et al 2008), cellulose, XAD-amberlites, sulfides, c-alumina (intermediate crystalline form of Al 2 O 3 ), bentonite (Spagna et al 1995) and CIM-disk epoxy monolith [epoxy columns composed of a disk of methacrylatebased porous polymer matrix a non-porous (monolith) (Delattre et al 2008). Most research on immobilization has been carried out using commercial enzyme mixtures for the co-immobilization of pectinolytic enzymes (Vaillant et al 2000;Diano et al 2008).…”