ArticleApplied biochemistry and biotechnology2024
Hydrolysis of Casein by Pepsin Immobilized on Heterofunctional Supports to Produce Antioxidant Peptides.
Article in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Immobilized enzymes: exploring its potential in food industry applications.Food science and biotechnology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
A study was carried out on the immobilization of pepsin in activated carbon functionalized by different techniques (glutaraldehyde, genipin, and metallization) aiming at its application in obtaining bioactive peptides through casein hydrolysis. Studies of the immobilized derivatives were carried out in addition to the evaluation of the antioxidant potential of the peptides. Among the pH range studied, pH 3.0 was selected due to the higher activity of the derivatives at this pH. The support modification by metallization was the method with the best results, providing a 121% increase in enzymatic activity compared to other immobilization methods. In addition, this derivative provided activity closer to the soluble enzyme activity (3.30 U) and better storage stability, and allows reuse for more than 8 cycles. In turn, the peptides from casein hydrolysis showed potential as antioxidant agents, with a DPPH radical scavenging activity higher than 70%, maximum protection against β-carotene oxidation close to 70%, and a maximum reducing power of Fe(III) into Fe(II) of 400 uM by the FRAP assay. The results showed that the new techniques for modification of activated carbon can be a promising approach for pepsin immobilization.
Indexed as
Identifiers
38888698What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.