Response surface optimization of enzymatic hydrolysis and ROS scavenging activity of silk sericin hydrolysates.
Alcalase®
RSM
Waste product
antioxidant
Journal
Pharmaceutical biology
ISSN: 1744-5116
Titre abrégé: Pharm Biol
Pays: England
ID NLM: 9812552
Informations de publication
Date de publication:
Dec 2022
Dec 2022
Historique:
entrez:
11
2
2022
pubmed:
12
2
2022
medline:
5
3
2022
Statut:
ppublish
Résumé
Sericin, a protein found in wastewater from the silk industry, was shown to contain a variety of biological activities, including antioxidant. The enzymatic conditions have been continuously modified to improve antioxidant effect and scavenging capacity against various free radicals of silk sericin protein. Variables in enzymatic reactions, including pH, temperature and enzyme/substrate ratio were analysed to discover the optimum conditions for antioxidant activity of sericin hydrolysates. Hydrolysis reaction catalysed by Alcalase Among these three variables, response surface plots demonstrate the major role of temperature on scavenging capacity of sericin hydrolysates. Sericin hydrolysates prepared by using Alcalase The acquired RSM information would be of benefit for further developing antioxidant peptide from diverse resources, especially the recycling of waste products from silk industry.
Identifiants
pubmed: 35148231
doi: 10.1080/13880209.2022.2032208
pmc: PMC8843116
doi:
Substances chimiques
Antioxidants
0
Free Radical Scavengers
0
Reactive Oxygen Species
0
Sericins
0
Subtilisins
EC 3.4.21.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
308-318Références
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