Fractionation of the proteolytic and amylolytic complex enzyme system of streptomyces aureofaciens and some properties of fractions

Biotechnology and Bioengineering
C Laluce, R Molinari

Abstract

The Streptomyces aureofaciens extracellular proteolytic system was split into four fractions by carboxymethylcellulose (CMC) column chromatography giving three purely caseinolytic fractions and one fraction active toward both starch and casein. The first caseinolytic and amylolytic fraction was further fractionated by DEAE-Sephadex A-50 chromatography into one purely amylolytic fraction and another showing both activities, was refractioned into four new fractions by DEAE-cellulose chromatography. These fractions were found to be heterogeneous by polyacrylamide gel electrophoresis, three of them acted on both starch and casein and a fourth was only caseinolytic. The second CMC fraction was further purified by CMC rechromatography to an homogeneous fraction that hydrolyzes carboxypeptidase A(EC 3.4.2.1) synthetic substrates and solubilizes elastin. It had only one polypeptide chain with a molecular weight of about 28000 daltons, a high thermal stability in the presence of calcium ions, a pH optimum of about 6.8, and a maximal caseinolytic activity at about 50 degrees C.

References

Jan 1, 1970·The Biochemical Journal·M Trop, Y Birk
Jul 1, 1966·Archives of Biochemistry and Biophysics·B F ERLANGERA G Cooper
Jan 1, 1961·The Biochemical Journal·M A NAUGHTON, F SANGER
Nov 1, 1961·Archives of Biochemistry and Biophysics·B F ERLANGERW COHEN
Mar 20, 1947·The Journal of General Physiology·M Kunitz

Related Concepts

Amylose
Casein A
Chromatography
Chromatography, DEAE-Cellulose
Ion-Exchange Chromatography Procedure
SDS-PAGE
Chemical Fractionation
Hydrolysis
Peptide Hydrolases
Streptomyces aureofaciens

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