The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Improvement of enzyme activity, stability and selectivity via immobilization techniques
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2007.01.018 · Cited by 3,375
Durán, N., Rosa, M. A., D’Annibale, A., & Gianfreda, L. (2002) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(02)00214-4 · Cited by 629
Betancor, L., López-Gallego, F., Hidalgo, A., Alonso-Morales, N., Mateo, G. D.-O. C., Fernández-Lafuente, R., & Guisán, J. M. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.01.014 · Cited by 414
Immobilization of peroxidases on glass beads: An improved alternative for phenol removal
Gómez, J. L., Bódalo, A., Gómez, E., Bastida, J., Hidalgo, A. M., & Gómez, M. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.02.008 · Cited by 171
Chang, M.-Y., & Juang, R. (2004) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2004.06.013 · Cited by 149
Use of chemically modified PMMA microspheres for enzyme immobilization
Li, S., Hu, J., & Liu, B. (2004) · Biosystems · doi:10.1016/j.biosystems.2004.03.001 · Cited by 100
Immobilization of horseradish peroxidase onto polyaniline polymers
Fernandes, K. F., Lima, C. S., Pinho, H., & Collins, C. H. (2003) · Process Biochemistry · doi:10.1016/s0032-9592(03)00021-9 · Cited by 90
Glucoamylase, α-amylase and β-amylase immobilisation on acrylic carriers
Bryjak, J. (2003) · Biochemical Engineering Journal · doi:10.1016/s1369-703x(03)00114-1 · Cited by 88
Treatment of phenolic wastewater by horseradish peroxidase immobilized by bioaffinity layering
Dalal, S., & Gupta, M. N. (2006) · Chemosphere · doi:10.1016/j.chemosphere.2006.10.043 · Cited by 88
Research works printed but not linked: 4
Cited by
Routoula, E., & Patwardhan, S. V. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b03737 · Cited by 579
Horseradish peroxidase (HRP) as a tool in green chemistry
Lopes, G. R., Pinto, D. C. G. A., & Silva, A. M. S. (2014) · RSC Adv. · doi:10.1039/c4ra06094f · Cited by 154
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)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
