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Purification of an Aspartic Proteinase from Aspergillus Aculeatus

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Structure and Function of the Aspartic Proteinases

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 306))

Abstract

Aspergilli are known to produce a number of extracellular enzymes (e.g. proteinases, carbohydrases, lipases). Several are utilized in commercial products, based on a main activity, but often containing minor side activities. Usually it is difficult to isolate small amounts of a side activity, but in such cases affinity chromatography can be a valuable tool, due to its specific action. We have succeeded in isolating a proteolytic side activity from the Aspergillus aculeatus derived carbohydrase product Viscozyme™ (Novo Nordisk A/S, Denmark). The proteinase was isolated by affinity chromatography on a bacitracin matrix, and was shown to be an aspartic proteinase.

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© 1991 Plenum Press, New York

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Mortensen, S.B., Dambmann, C. (1991). Purification of an Aspartic Proteinase from Aspergillus Aculeatus . In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_30

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  • DOI: https://doi.org/10.1007/978-1-4684-6012-4_30

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-6014-8

  • Online ISBN: 978-1-4684-6012-4

  • eBook Packages: Springer Book Archive

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