Biochemical Properties of a Partially Purified Protease from Bacillus sp. CL18 and Its Use to Obtain Bioactive Soy Protein Hydrolysates.
Bioactivity
Biocatalysis
Characterization
Enzyme
Protein hydrolysate
Thermal inactivation
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Oct 2020
Oct 2020
Historique:
received:
28
02
2020
accepted:
22
05
2020
pubmed:
7
6
2020
medline:
29
4
2021
entrez:
7
6
2020
Statut:
ppublish
Résumé
Microbial proteases are relevant biocatalysts with diverse applications. Production of protein hydrolysates is recently focused, since they might display biological activities. Therefore, the extracellular protease from Bacillus sp. CL18 was partially purified through ammonium sulfate precipitation (25-50% saturation) and gel filtration chromatography, with a 60.7-fold purification (40,593 U/mg protein) and 21.3% recovery. The partially purified protease (PPP) was characterized as a serine protease, with optimal activity at 51-59 °C and pH 7.4-8.8 and low thermal stability. Thermal inactivation followed first-order kinetics. PPP depended on Ca
Identifiants
pubmed: 32504245
doi: 10.1007/s12010-020-03355-1
pii: 10.1007/s12010-020-03355-1
doi:
Substances chimiques
Angiotensin-Converting Enzyme Inhibitors
0
Dipeptidyl-Peptidase IV Inhibitors
0
Protein Hydrolysates
0
Soybean Proteins
0
Peptide Hydrolases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
643-664Subventions
Organisme : Conselho Nacional de Desenvolvimento Científico e Tecnológico
ID : 402631/2016-1