Purification and characterization of chitinase produced by thermophilic fungi
Anion exchange chromatography
SDS-PAGE
chitinase
enzyme kinetics
purification
Journal
Preparative biochemistry & biotechnology
ISSN: 1532-2297
Titre abrégé: Prep Biochem Biotechnol
Pays: England
ID NLM: 9607037
Informations de publication
Date de publication:
2022
2022
Historique:
pubmed:
4
2
2022
medline:
5
10
2022
entrez:
3
2
2022
Statut:
ppublish
Résumé
In the past few years, the production of shrimp shell waste from the seafood processing industries has confronted a significant surge. Furthermore, insignificant dumping of waste has dangerous effects on both nature and human well-being. This marine waste contains a huge quantity of chitin which has several applications in different fields. The chitinase enzyme can achieve degradation of chitin, and the chitin itself can be used as the substrate as well for production of chitinase. In the current study, the chitinase enzyme was produced by The chitinase activity was found to be highest at pH 6.5, 50 °C, and 60 min after the reaction began. and the chitinase showed the highest activity and stability in the presence of β-mercaptoethanol (ME). The SDS-PAGE of denatured purified chitinase showed a protein band of 18 kDa. The characterization study concludes that Cu
Sections du résumé
BACKGROUND
UNASSIGNED
In the past few years, the production of shrimp shell waste from the seafood processing industries has confronted a significant surge. Furthermore, insignificant dumping of waste has dangerous effects on both nature and human well-being. This marine waste contains a huge quantity of chitin which has several applications in different fields. The chitinase enzyme can achieve degradation of chitin, and the chitin itself can be used as the substrate as well for production of chitinase. In the current study, the chitinase enzyme was produced by
RESULT
UNASSIGNED
The chitinase activity was found to be highest at pH 6.5, 50 °C, and 60 min after the reaction began. and the chitinase showed the highest activity and stability in the presence of β-mercaptoethanol (ME). The SDS-PAGE of denatured purified chitinase showed a protein band of 18 kDa.
CONCLUSION
UNASSIGNED
The characterization study concludes that Cu
Identifiants
pubmed: 35112660
doi: 10.1080/10826068.2022.2028639
doi:
Substances chimiques
Complex Mixtures
0
Ions
0
Chitin
1398-61-4
Mercaptoethanol
60-24-2
DEAE-Cellulose
9013-34-7
Edetic Acid
9G34HU7RV0
Chitinases
EC 3.2.1.14
Mercury
FXS1BY2PGL
Ammonium Sulfate
SU46BAM238
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM