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Purification and partial characterization of a proteolytic enzyme from Cephalosporium acremonium (Corda)

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Abstract

A proteolytic enzyme was isolated fromCephalosporium acremonium (Corda). The enzyme had a molecular weight of 28,200 and a pH optimum of 8.4–9.2. Proteolytic activity was inhibited by diisopropylfluorophosphate and mercuric chloride. Of the substrates tested, casein was most rapidly hydrolyzed.

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Authors and Affiliations

  1. Antibiotic Manufacturing and Development Division Eli Lilly & Co., Indianapolis, Ind.

    F. M. Huber

Authors
  1. F. M. Huber
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  2. P. A. Barnwell
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  3. R. H. Baltz
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Huber, F.M., Barnwell, P.A. & Baltz, R.H. Purification and partial characterization of a proteolytic enzyme from Cephalosporium acremonium (Corda). Mycopathologia et Mycologia Applicata 44, 149–157 (1971). https://doi.org/10.1007/BF02051883

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