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2000
DOI: 10.1023/a:1005601607277
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Cited by 35 publications
(14 citation statements)
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“…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
confidence: 88%
“…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
confidence: 88%
“…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].…”
Section: Effect On Kinetic Parameterssupporting
confidence: 85%
“…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.…”
Section: Resultsmentioning
confidence: 87%