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Studies on the activity and stability of immobilized horseradish peroxidase on poly(ethylene terephthalate) grafted acrylamide fiber
Abstract
Having been activated with glutaraldehyde, modified poly(ethylene terephthalate) grafted acrylamide fiber was used for the immobilization of horseradish peroxidase (HRP). Both the free HRP and the immobilized HRP were characterized by determining the activity profile as a function of pH, temperature, thermal stability, effect of organic solvent and storage stability. The optimum pH values of the enzyme activity were found as 8 and 7 for the free HRP and the immobilized HRP respectively. The temperature profile of the free HRP and the immobilized HRP revealed a similar behaviour, although the immobilized HRP exhibited higher relative activity in the range from 50 to 60 degrees C. The immobilized HRP showed higher storage stability than the free HRP.
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“Majority of examples examined are using lengthy synthesis procedures with many subsequent steps for the materials synthesis and the immobilisation of the enzyme, and further hazardous chemicals and unsustainable practices are usually employed 189, 192, 196, 197, 199, 222-224 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [222]
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Metadata
- Authors
- Temoçin, Z., & Yiğitoğlu, M.
- Venue
- Bioprocess and Biosystems Engineering
- Published
- 2008-10-14
- Volume
- 32
- Issue
- 4
- Pages
- 467-474
- ISSN
- 1615-7591
- 1615-7605
- Cited by
- 65
- References
- 40
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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