Characterization of a novel aspartic protease from Trichoderma asperellum for the preparation of duck blood peptides.
Aspartic protease
Biochemical characterization
Duck blood peptides
Komagataella phaffii
Trichoderma asperellum
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Dec 2024
Dec 2024
Historique:
received:
02
05
2023
accepted:
01
12
2023
revised:
24
11
2023
medline:
17
1
2024
pubmed:
17
1
2024
entrez:
17
1
2024
Statut:
ppublish
Résumé
A novel aspartic protease gene (TaproA1) from Trichoderma asperellum was successfully expressed in Komagataella phaffii (Pichia pastoris). TaproA1 showed 52.8% amino acid sequence identity with the aspartic protease PEP3 from Coccidioides posadasii C735. TaproA1 was efficiently produced in a 5 L fermenter with a protease activity of 4092 U/mL. It exhibited optimal reaction conditions at pH 3.0 and 50 °C and was stable within pH 3.0-6.0 and at temperatures up to 45 °C. The protease exhibited broad substrate specificity with high hydrolysis activity towards myoglobin and hemoglobin. Furthermore, duck blood proteins (hemoglobin and plasma protein) were hydrolyzed by TaproA1 to prepare bioactive peptides with high ACE inhibitory activity. The IC
Identifiants
pubmed: 38229301
doi: 10.1007/s00253-023-12848-y
pii: 10.1007/s00253-023-12848-y
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
131Subventions
Organisme : National Natural Science Foundation of China
ID : 32272913
Informations de copyright
© 2024. The Author(s).
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