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Metabolism and Products

Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae

A. K. Kundu, S. Manna
A. K. Kundu
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S. Manna
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DOI: 
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This article has a correction. Please see:

  • Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae
    - December 01, 1983

ABSTRACT

The extracellular proteinases of Aspergillus oryzae EI 212 were separated into two active fractions by (NH4)2SO4 and ethanol fractionation followed by diethyl-aminoethyl-Sephadex A-50 and hydroxyapatite chromatography. The molecular weight was estimated by gel filtration to be about 70,000 and 35,000 for proteinases I and II, respectively. Optimum pH for casein and hemoglobin hydrolysis was 6.5 at 60 C for proteinase I and 10.0 at 45 C for proteinase II, and for gelatin hydrolysis it was 6.5 at 45 C for both enzymes. The enzymes were stable over the pH range 6 to 8 at 30 C for 60 min. The enzyme activity for both the proteinases was accelerated by Cu2+ and inhibited by Fe2+, Fe3+, Hg2+, and Ag+. Halogenators (e.g., N-chlorosuccinimide) and diisopropyl fluorophosphate inhibited proteinase II. Sulfhydryl reagents such as p-chloromercuribenzoate and iodoacetate inhibited proteinase I. Sulfhydryl compounds accelerated the action of both enzymes.

  • Copyright © 1975 American Society for Microbiology
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Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae
A. K. Kundu, S. Manna
Applied Microbiology Oct 1975, 30 (4) 507-513; DOI:

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Purification and Characterization of Extracellular Proteinases of Aspergillus oryzae
A. K. Kundu, S. Manna
Applied Microbiology Oct 1975, 30 (4) 507-513; DOI:
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