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- W3119489000 abstract "An industrially important enzyme, Candida antarctica lipase B (CalB), was modified with a range of functional polymers including hydrophilic, hydrophobic, anionic, and cationic character using a “grafting to” approach. We determined the impact of polymer chain length on CalB activity by synthesizing biohybrids of CalB with each polymer at three different chain lengths, using reversible addition-fragmentation chain transfer (RAFT) polymerization. The activity of CalB in both aqueous and aqueous-organic media mixtures was significantly enhanced for acrylamide (Am) and N,N-dimethyl acrylamide (DMAm) conjugates, with activity remaining approximately constant in 25 and 50% ethanol solvent systems. Interestingly, the activity of N,N-dimethylaminopropyl-acrylamide (DMAPA) conjugates increased gradually with increasing organic solvent content in the system. Contrary to other literature reports, our study showed significantly diminished activity for hydrophobic polymer-protein conjugates. Functional thermal stability assays also displayed a considerable enhancement of retained activity of Am, DMAm, and DMAPA conjugates compared to the native CalB enzyme. Thus, this study provides an insight into possible advances in lipase production, which can lead to new improved lipase bioconjugates with increased activity and stability." @default.
- W3119489000 created "2021-01-18" @default.
- W3119489000 creator A5024656274 @default.
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- W3119489000 creator A5082255853 @default.
- W3119489000 date "2021-01-08" @default.
- W3119489000 modified "2023-10-16" @default.
- W3119489000 title "Polymer Modification of Lipases, Substrate Interactions, and Potential Inhibition" @default.
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- W3119489000 doi "https://doi.org/10.1021/acs.biomac.0c01159" @default.
- W3119489000 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33416313" @default.
- W3119489000 hasPublicationYear "2021" @default.
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