Submerged Production, Purification, and Crystallization of Acid Carboxypeptidase from Penicillium janthinellum IFO-8070
AUTOR(ES)
Yokoyama, Sadaji
RESUMO
Penicillium janthinellum IFO-8070 produced an acid carboxypeptidase of molecular weight 51,000 in a liquid medium at 25 C. Maximum enzyme concentration was obtained within 3 to 6 days in a medium containing 2% wheat bran, 1% defatted soybean, and 1% KH2PO4; the initial pH was 2 to 4. When submerged aerobic conditions were used, a 51,000-molecular-weight acid carboxypeptidase was produced and no detectable amounts of 160,000-molecular-weight acid carboxypeptidase were produced. Acid carboxypeptidase with a molecular weight of 51,000 was purified 330-fold from koji culture to yield a crystalline protein which was demonstrated by disc electrophoresis to be homogeneous. The purification method included ammonium sulfate fractionation, Amberlite CG-50 chromatography, acetone fractionation, Amberlite CG-50 rechromatography, and concentration in a collodion bag. The specific activity of the enzyme was about three times more than that of the acid carboxypeptidase from Aspergillus saitoi.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=186817Documentos Relacionados
- Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09
- Production, Purification, and Characterization of α-Galactosidase from Monascus pilosus
- Production, purification, and characterization of an extracellular chitosanase from Streptomyces.
- Production, purification, and characterization of alpha-amylase from Thermomonospora curvata.
- PRODUCTION, PURIFICATION, AND CHARACTERIZATION OF SYNNEMATIN1