Your browser doesn't support javascript.
loading
Thermostable alkaline metalloprotease from newly isolated alkalophilic Streptomyces diastaticus strain SS1.
Indian J Biochem Biophys ; 1998 Feb; 35(1): 34-40
Article Dans Anglais | IMSEAR | ID: sea-28553
ABSTRACT
Thermostable alkaline metalloprotease (EC 3.4.24.4), a simple protein of very low molecular mass (11 kDa), was isolated and purified from the cell free broth of Streptomyces diastaticus sp SS1 by concentration, (NH4)2SO4 precipitation and affinity chromatography over casein. The isoelectric point of the protease is 7.2. The temperature and pH optima for the enzyme activity are 37 degrees C and 8 respectively. The half life of the enzyme at 55 degrees C is 24 hr and the enzyme is stable over a pH range of 7.5 to 9. The K(m) value of the enzyme was estimated to be 2 x 10(-3) mg ml-1. Ca2+ is essential for enzyme activity as well as thermal stability. The alpha-helix content of the metalloprotease is calculated to be 50% from the circular dichroism spectrum. The number of Zn2+ binding to each molecule of protease is determined to be one by atomic absorption.
Sujets)
Texte intégral: Disponible Indice: IMSEAR (Asie du Sud-Est) Sujet Principal: Streptomyces / Température / Stabilité enzymatique / Metalloendopeptidases / Alcalis langue: Anglais Texte intégral: Indian J Biochem Biophys Année: 1998 Type: Article

Documents relatifs à ce sujet

MEDLINE

...
LILACS

LIS

Texte intégral: Disponible Indice: IMSEAR (Asie du Sud-Est) Sujet Principal: Streptomyces / Température / Stabilité enzymatique / Metalloendopeptidases / Alcalis langue: Anglais Texte intégral: Indian J Biochem Biophys Année: 1998 Type: Article