Abstract
Methods for characterization of protease activity were applied to three Bacillus sp. protease preparations of varying purity. Activities differed by several orders of magnitude between the three proteases. Fractionation by HPLC and assay of peak activity against the two substrates elucidated the presence of 1–4 active fractions in each protease preparation.
Similar content being viewed by others
References
Bergmeyer U (1983) Enzymes 3: Peptidases, Proteinases and their Inhibitors. Deerfield Beach: Verlag Chemie GmbH.
Beynon R, Bond J (2001) Proteolytic Enzymes: The Practical Approach Series. Oxford: Oxford University Press.
Iversen S, Jorgensen M(1995) Azocasein assay for alkaline protease in complex fermentation broth. Biotechnol. Tech. 9: 573-576.
Jenness R, Koops J (1962) Preparation and properties of a salt solution which simulates milk ultrafiltrate. Neth. Milk Dairy J. 16: 153-164.
Keil B (1992) Specificity of Proteolysis. Berlin: Springer-Verlag.
Schumaker G, Schill W (1972) Radial diffusion in gel for micro determination of enzymes. II. Plasminogen activator, elastase, and nonspecific proteases. Anal. Biochem. 48: 9-26.
Siezen R, Leunissen J (1997) Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6: 501-523.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bjurlin, M.A., Bloomer, S. & Nelson, C.J. Characterization of proteolytic activity of proteases. Biotechnology Letters 24, 191–195 (2002). https://doi.org/10.1023/A:1014153122933
Issue Date:
DOI: https://doi.org/10.1023/A:1014153122933