“…Among the heterogeneous systems, micro-encapsulated HRPs were more reactive than the Eupergit-supported enzyme, and HRPm/LbL was the best catalyst (56 % degradation yield after In accordance with data reported previously, [31] there is the possibility of residual un-reacted oxirane groups on Eupergit C 250 L, which would allow it to interact with dye molecules. The treatment of HRP/E-LbL with ethanolamine during the preparation of the catalyst was probably not sufficient to eliminate these secondary reactions.…”
Section: Oxidation Of Dyes With Hrp/elbl Hrpm/lbl and Hrpm/ Lblp Catsupporting
Abstract3,4‐Dihydroxyphenylalanine (DOPA)‐containing peptides and proteins provide attractive design paradigms for pharmaceutical applications and engineering of synthetic polymers. An efficient and selective route to DOPA peptides by oxidation of L‐tyrosine derivatives with tyrosinase is reported. The efficiency of the procedure was tested by using successively recycled tyrosinase immobilized on Eupergit®C250L and coated with polyelectrolytes by the layer‐by‐layer method.
“…Among the heterogeneous systems, micro-encapsulated HRPs were more reactive than the Eupergit-supported enzyme, and HRPm/LbL was the best catalyst (56 % degradation yield after In accordance with data reported previously, [31] there is the possibility of residual un-reacted oxirane groups on Eupergit C 250 L, which would allow it to interact with dye molecules. The treatment of HRP/E-LbL with ethanolamine during the preparation of the catalyst was probably not sufficient to eliminate these secondary reactions.…”
Section: Oxidation Of Dyes With Hrp/elbl Hrpm/lbl and Hrpm/ Lblp Catsupporting
Abstract3,4‐Dihydroxyphenylalanine (DOPA)‐containing peptides and proteins provide attractive design paradigms for pharmaceutical applications and engineering of synthetic polymers. An efficient and selective route to DOPA peptides by oxidation of L‐tyrosine derivatives with tyrosinase is reported. The efficiency of the procedure was tested by using successively recycled tyrosinase immobilized on Eupergit®C250L and coated with polyelectrolytes by the layer‐by‐layer method.
“…This indicates that the immobilization results in lowering the affinity for the substrate with respect to free enzyme. Around 2.5-fold increase in K m value after immobilization was also reported earlier [34].…”
The different ionic molecules/compounds were used as a ligand for the immobilization of penicillin G acylase on the highly porous cellulose-based polymeric membrane having buffer flux 1,746 LMH (L m(-2) h(-1)) at 0.5 bar pressure. The immobilized enzyme activity around 250 U(App) was obtained with the ligand such as proline, tryptophan, casein acid hydrolysate, and brilliant green. Comparatively, proline showed less IMY% (percentage immobilization yield--58) but higher RTA% (percentage of activity retention--71) and specific activity (145 U(App) g(-1)). However, the crosslinked preparation of brilliant green obtained using glutaraldehyde showed 82 +/- 2.7% immobilized enzyme activity after the completion of successive five cycles. In comparison with the free enzyme, the enzyme immobilized on the brilliant green coupled membrane showed around 2.4-fold increase in K (m) value (47.4 mM) as well as similar optimum pH (7.2) and temperature (40 degrees C). The immobilized enzyme retained almost 50% activity after 107 days and 50 cycles of operation. Almost 50% decrease in buffer flux after enzyme immobilization was observed. At the end of the 30 cycles, flux pattern shows around 38% decrease in buffer flux however, after 16 cycles of operation flux moves closer towards the steady state.
“…Recently, similar results were reported for the K m values of free and immobilized glucose isomerase on Eupergit C, were 423 and 2602 mM respectively. 16) This type of change has also been observed in the immobilization of dextranase on Eupergit C, which showed 33% of the catalytic efficiency of the native enzyme. The decreased catalytic efficiency of BLAI after covalent immobilization on Eupergit C is consistent with previous reports on immobilization of several enzymes.…”
Section: Characterization Of the Blai Immobilized On Eupergit Cmentioning
confidence: 62%
“…For example, for lipase or penicillin acylase, enzyme loading was 100 mg/g 15) and 40 mg/g support 12) respectively. Compared with these two enzymes, the enzyme loading of BLAI was low, but was higher than that of penicillin V acylase (1 mg/g of support), 16) and was similar to that of glucose isomerase. 17) The other two main factors in immobilization, temperature and pH, were employed in the CCD design to investigate their effects and the interactions between them.…”
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