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• W416763942 abstract "Effect of pegylation on the activities and stabilities of horseradish peroxidase (HRP) and n-carbamoyl-l-amino acid amidohydrolase (l-N-carbamoylase) was investigated. Pegylation was favored under alkaline conditions with high PEG/enzyme molar ratios. The lysine residues in l-N-carbamoylase were found to be more readily accessible for pegylation than those in HRP, leading to the formation of multi-pegylated enzymes. Pegylation and addition of mPEG as an additive improved HRP activity by 64% and 42%, respectively, via the formation of protective layers against the free radical-induced inactivation. The activity of pegylated l-N-carbamoylase, however, declined due to the additional mass transfer resistance introduced by the PEG layers. The extent of reduction in l-N-carbamoylase activity increased with the level of pegylation. In terms of thermostability, both the addition of mPEG as an additive and pegylation with PEG5000 led to a decline in thermostability. Nevertheless, pegylation of HRP with PEG2000 resulted in a PEG-HRP conjugate exhibiting a thermostability two-fold that of the control at 70 °C, probably due to the capability of the relatively hydrophilic PEG domains on the conjugate in avoiding enzyme aggregation. After a 4-day incubation at room temperature, pegylated HRP retained significantly higher activity, 89%, than the control, 12%." @default.
• W416763942 created "2016-06-24" @default.
• W416763942 creator A5039556188 @default.
• W416763942 creator A5053774575 @default.
• W416763942 date "2015-09-01" @default.
• W416763942 modified "2023-09-26" @default.
• W416763942 title "Effect of PEGylation on the activity and stability of horseradish peroxidase and l-N-carbamoylase in aqueous phases" @default.
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• W416763942 doi "https://doi.org/10.1016/j.procbio.2015.04.024" @default.
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