Applied Biochemistry and Biotechnology

, Volume 37, Issue 3, pp 283–294 | Cite as

Purification and Characterization of a Milk Clotting Protease fromMucor bacilliformis

  • Liliana B. Areces
  • Mirtha Biscoglio De Jiménez Bonino
  • Marina A. A. Parry
  • Elda R. Fraile
  • Héctor M. Fernández
  • Osvaldo Cascone


An acid protease having milk clotting activity has been isolated fromMucor bacilliformis cultures. The enzyme was basically purified by ionic exchange chromatography. An average yield of 29 mg purified product was obtained from 100 mL crude extract. As purity criteria, SDS-PAGE, reverse-phase HPLC, and N-terminal analysis were performed. The protease is a protein composed of a single polypeptide chain with glycine at the N-terminus. The mol wt is approx 32,000, and its amino acid composition is very similar to those of other fungal proteases. As expected, its clotting activity was drastically inhibited by pepstatin A action. On the other hand, its instability against heat treatment and its clotting/proteolytic activity ratio indicate that it may be considered as a potential substitute for bovine chymosin. Index Entries:Mucor bacilliformis protease; milk clotting enzyme; acid protease; fungal protease; aspartyl protease.


Apply Biochemistry Proteolytic Activity Wheat Bran Mucor Clotting Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© The Humana Press Inc 1993

Authors and Affiliations

  • Liliana B. Areces
    • 1
  • Mirtha Biscoglio De Jiménez Bonino
    • 1
  • Marina A. A. Parry
    • 1
  • Elda R. Fraile
    • 2
  • Héctor M. Fernández
    • 2
  • Osvaldo Cascone
    • 2
  1. 1.Institute de Quimica y Fisicoquimica Biológicas (UBA-CONICET)Universidad de Buenos AiresBuenos AiresArgentina
  2. 2.Cátedra de Microbiologia Industrial y Biotecnologia, Facultad de Farmacia y BioquimicaUniversidad de Buenos AiresBuenos AiresArgentina

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