Characterization of an intracellular aspartic protease (PsAPA) from Penicillium sp. XT7 and its application in collagen extraction.
Characterization
Collagen extraction
Intracellular aspartic protease
Penicillium sp.
Yield
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 May 2021
30 May 2021
Historique:
received:
12
07
2020
revised:
09
11
2020
accepted:
03
12
2020
pubmed:
22
12
2020
medline:
11
3
2021
entrez:
21
12
2020
Statut:
ppublish
Résumé
An intracellular aspartic protease, PsAPA, was identified from Penicillium sp. XT7. This protease was belonged to penicillopepsin and was expressed in Pichia pastoris GS115. The recombinant PsAPA had a specific activity of 4289.7 ± 261.7 U/mg. The pH and temperature maxima of the enzyme were 3.0 and 30 °C, respectively. The PsAPA was stable in the pH range from 3.0 to 6.0 and was completely inactivated after incubation at 50 °C for 15 min. Presence of Mn
Identifiants
pubmed: 33348133
pii: S0308-8146(20)32696-0
doi: 10.1016/j.foodchem.2020.128834
pii:
doi:
Substances chimiques
Collagen
9007-34-5
Aspartic Acid Proteases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
128834Informations de copyright
Copyright © 2020. Published by Elsevier Ltd.