Premium
Isolation and characterization of a microbial Arg/Lys carboxypeptidase, carboxypeptidase F
Author(s) -
Matsumura E.,
Sato T.,
Toyoda N.
Publication year - 1995
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1995.tb00415.x
Subject(s) - carboxypeptidase , enzyme , arginine , lysine , biochemistry , carboxypeptidase a , chemistry , peptide , enzyme assay , amino acid
Carboxypeptidase F was isolated from a fungal strain F‐33 and characterized. The enzyme has the ability to release arginine and lysine from the carboxy terminus of peptides, and showed high specific activity against arginine (140 units mg ‐1 protein). Optimal temperature and pH for the enzyme reaction were 55°C and pH 8.5, respectively. The enzyme possessed a high thermal stability. Native molecular weight was estimated to be approximately 450000. Enzymatic activity was inhibited by Co 2+ , Cd 2+ , chelating agents and thiol inhibitors.