Tailored chitosan integration in diatomaceous earth particles as a scaffold for fructosyltransferase immobilization in fructo-oligosaccharide production.
Fructo‐oligosaccharides
covalently immobilization
diatomaceous earth particles
fructosyltransferase
Journal
Journal of the science of food and agriculture
ISSN: 1097-0010
Titre abrégé: J Sci Food Agric
Pays: England
ID NLM: 0376334
Informations de publication
Date de publication:
23 Mar 2024
23 Mar 2024
Historique:
revised:
13
03
2024
received:
05
01
2024
accepted:
21
03
2024
medline:
23
3
2024
pubmed:
23
3
2024
entrez:
23
3
2024
Statut:
aheadofprint
Résumé
Fructo-oligosaccharide (FOS) belongs to the group of short inulin-type fructans and is one of the most important non-digestible bifido-oligosaccharides capable of biotransforming sucrose using fructosyltransferases (FTase). However, there are no immobilized FTase products that can be successfully used industrially. In this study, diatomite was subjected to extrusion, sintering, and granulation to form diatomaceous earth particles that were further modified via chitosan aminomethylation for modification. FTase derived from Aspergillus oryzae was successfully immobilized on the modified support via covalent binding. The immobilized enzyme activity was 503 IU g Our results suggest that immobilized FTase as a viable candidate for continuous FOS production on an industrial scale. This article is protected by copyright. All rights reserved.
Sections du résumé
BACKGROUND
BACKGROUND
Fructo-oligosaccharide (FOS) belongs to the group of short inulin-type fructans and is one of the most important non-digestible bifido-oligosaccharides capable of biotransforming sucrose using fructosyltransferases (FTase). However, there are no immobilized FTase products that can be successfully used industrially. In this study, diatomite was subjected to extrusion, sintering, and granulation to form diatomaceous earth particles that were further modified via chitosan aminomethylation for modification. FTase derived from Aspergillus oryzae was successfully immobilized on the modified support via covalent binding.
RESULTS
RESULTS
The immobilized enzyme activity was 503 IU g
CONCLUSIONS
CONCLUSIONS
Our results suggest that immobilized FTase as a viable candidate for continuous FOS production on an industrial scale. This article is protected by copyright. All rights reserved.
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
This article is protected by copyright. All rights reserved.