Abstract
Aspartic proteinases are widely spread in most organisms, where they carry out many different functions. The oldest and most well–known use of aspartic proteinases is as coagulants in cheese–making. The coagulants are probably still the only commercial products containing aspartic proteinases as the active substance. The main commercial interest in coagulants is focused on how to enhance the enzyme activity and its performance during cheese–making. In contrast to this, most commercial interests in other aspartic proteinases deal with how to inhibit their activity in order to control their function. The main commercial coagulants can be divided into three groups according to their origin, animal rennet, fermentation produced chymosin (FPC) and microbial coagulants.1 Of animal rennets, calf rennet is the traditional and the most desired coagulant for cheese–making, but FPC products made by recombinant organisms and microbial coagulants, the natural aspartic proteinases of the fungi, make up a considerable part of the coagulant market. Fermentation produced chymosin is the product of the future, and the great interest in microbial coagulants is due to the fact that they constitute a significant part of the market because of their lower prices. Rhizomucor miehei aspartic proteinase (EC 3.4.23.23) constitutes the active component of the most widely used microbial coagulant. The molecule consists of 361 amino acids, has a molecular weight of 38701 and contains in addition approx. 6% carbohydrate.2 The enzyme is commercially available in its natural form, in various heat labile forms made by post-treatment of the natural form (oxidation) and as recombinant coagulant produced in Aspergillus oryzae.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Harboe, M. Coagulants of different origin. Eur. Dairy Magazine 2, 6–15, 1992.
Boel, E., Bech, A.-M, Randrup, K., Draeger, B., Fiil, N.P. and Foltmann, B. Primary structure of a precurser to the aspartic proteinase from Rhizomucor miehei shows that the enzyme is synthesized as a zymogen. Proteins: Structure, Function and Genetics 1:363–369, 1986.
International Dairy Federation. Bovine rennets. Determination of total milk–clotting activity. IDF Provisional Standard 157:1992.
PCT International Application. Microbially derived rennin having enhanced milk–clotting activity and method of producing same. WO 96/19582.
Gray, G.L:, Hayenga, K., Cullen, D., Wilson, L.J. and Norton, S. Primary structure of Mucor miehei aspar–tyl protease: evidence for a zymogen intermediate. Gene, 48, 41–53, 1986.
Aikawa, J., Yamashita, T., Nishiyama, M., Horinouchi, S. And Beppu, T. Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast. J. Biol. Chem., 265, 13955–13959, 1990.
Christensen, T., Woeldike, H., Boel, H., Mortensen, S.B., Hjortshoej, K., Thim, L. And Hansen, M.T. High level expression of recombinant genes in Aspergillus oryzae.. Biotechnology, 6, 1419–1422, 1988.
Zongchao, J., Vandonselaar, M., Schneider, P. and Quail, J.W. Crystallization and preliminary X–ray structure solution of Rhizomucor miehei aspartic proteinase. Acta Cryst. D51, 243–244, 1995.
Meldgaard, M. Glycosylation and stability of (l–3,l–4)–β–glucanases. Ph.D. Thesis November 1995, Carlsberg Laboratory and University of Copenhagen.
Foltmann, B. General and molecular aspects of rennets. Cheese: Chemistry, physics and microbiology (ed. P.F.Fox), vol 1,37–68, 1993.
Baudys, M., Erdene, G., Kostka, V., Pavlik, M. And Foltmann, B. Comparison between prochymosin and pepsinogen from lamb and calf.. Comp. Biochem. Physiol. Vol. 89B, No. 2. 385–391, 1988.
Baudys, M., Kostka, V. Covalent structure of chicken pepsinogen. Eur. J. Biochem. 136, 89–99, 1983.
Varki, A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology Vol. 3 no. 2, 97–130, 1993.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Harboe, M.K. (1998). Rhizomucor miehei Aspartic Proteinases Having Improved Properties. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_40
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5373-1_40
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7452-7
Online ISBN: 978-1-4615-5373-1
eBook Packages: Springer Book Archive