Peptidases from Maclura Pomifera for Preparation of Food Protein Hydrolysates: Purification by Single-Step Chromatography and Characterization of Pomiferin I.
Food protein hydrolysate
Maclura pomifera
Plant peptidase
Purification
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:
Mar 2021
Mar 2021
Historique:
received:
18
03
2020
accepted:
29
09
2020
pubmed:
14
10
2020
medline:
7
7
2021
entrez:
13
10
2020
Statut:
ppublish
Résumé
Our objective was to isolate peptidases from the latex of Maclura pomifera fruits and use them to hydrolyze food proteins, as well as to purify and characterize the main peptidase. Two partially purified proteolytic extracts were prepared by ethanol (EE) and acetone (AE) precipitation from an aqueous suspension of exuded fruit latex. EE was used to hydrolyze food proteins with a ratio of 0.19 caseinolytic units (Ucas) per mg of substrate. Different values of hydrolysis degree were observed for hydrolysates of egg white, soy protein isolate, and casein at 180 min (9.3%, 31.1%, and 29.1%, respectively). AE was employed to purify a peptidase which exhibited an isoelectric point (pI) of 8.70 and whose abundance in AE was 28.3%. This enzyme was purified to homogeneity using a single-step procedure by cation-exchange chromatography, achieving an 8.1-fold purification and a yield of 16.7%. The peptidase was named pomiferin I and showed a molecular mass of 63,177.77 Da. Kinetic constants (K
Identifiants
pubmed: 33047217
doi: 10.1007/s12010-020-03438-z
pii: 10.1007/s12010-020-03438-z
doi:
Substances chimiques
Dietary Proteins
0
Plant Proteins
0
Protein Hydrolysates
0
Peptide Hydrolases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
619-636Subventions
Organisme : UNLP
ID : X-746
Organisme : UNLP
ID : X-834
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