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Aguilar, C.F., Cronin, N.B., Badasso, M., Dreyer, T., Newman, M.P., Cooper, J.B., Hoover, D.J., Wood, S.P., Johnson, M.,S. and Blundell, T. (1997) The three-dimensional structure at 2.4Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae J. Mol. Biol. 267, 899–915.
Aikawa, J., Park, Y.N., Sugiyama, M., Nishiyama, M., Horinouchi, S. and Beppu, T. (2001) Replacement of amino acid residues at subsites and their effects on the catalytic properties of Rhizomucor pusillus pepsin, an aspartic proteinase from Rhizomucor pusillus. J. Biochem. 129, 791–794.
Aikawa, J., Yamashita, T., Nishiyama, M., Horinouchi, S. and Beppu, T. (1990) 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.
Andreeva, N. and Rumsh, L.D. (2001) Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes. Protein Sci. 10, 2439–2450.
Awad, S., Luthi-Peng, Q.Q. and Puhan, Z. (1999) Proteolytic activities of Suparen and Rennilase on buffalo, cow, and goat whole casein and beta-casein. J. Agric. Food Chem. 47, 3632–3639.
Blundell, T.L., Jenkins J.A., Sewell, B.T., Pearl, L.H., Cooper, J. B., Tickle, I.J., Veerapandian, B. and Wood, S.P. (1990) X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 Å resolution of endothiapepsin. J. Mol. Bio 941.
Branner-Jorgensen, S., Inventor; Branner-Jorgensen, S., assignee. (1981 March 10) Thermal destabilization of microbial rennet. U.S. Patent 4,255,454.
Branner-Jorgensen, S., Schneider, P. and Eigtved, P., inventors; Novo Industri A/S, assignee. (1982 November 2) Thermal destabilization of microbial rennet. U.S. Patent 4, 357, 357.
Budtz, P. and Heldt-Hansen, H. P., inventors; Gist-brocades, B. V., assignee. (1998 September 1) Cheese making with recombinant aspartic protease. U.S. Patent 5, 800, 849.
Castanheira, P., Samyn, B., Sergeant, K., Clemente, J.C., Dunn, B. M., Pires, E. Van Beeumen, J. and Faro., C. (2005) Activation, proteolytic processing, and peptide specificity of recombinant cardosin A. J. Biol. Chem. 280, 13047–13054
Chitpinitoyl, S. and Crabbe, M.J.C. (1998) Chymosin and aspartic proteinases. Food Chem. 61, 395–418.
Coates, L., Erskine, P.T., Crump, M.P., Wood, S.P. and Cooper, J.B. (2002) Five atomic resolution structures of endothiapepsin inhibitor complexes: Implications for the aspartic proteinase mechanism. J. Mol. Biol. 318, 1405–415.
Cooper, J.B., Khan, G., Taylor, G., Tickle, I.J. and Blundell, T. (1990) X-ray analysis of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 Å resolution. J. Mol. Biol. 214, 199–222.
Davies, D.R. (1990) The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Biophys. Chem. 19, 189–215.
Domingos, A., Cardoso, P.C., Xue, Z.T., Clemente, A., Brodelius, P.E. and Pais, M.S. (2000) Purification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa. Eur. J. Biochem. 267, 6824–6831.
Dunn-Coleman, N.S., Bloebaum, P., Berka, R.M., Bodie, E., Robinson, N., Armstrong, G., Ward, M., Przetak, M., Carter, G.L., LaCost, R., Wilson, L.J., Kodama, H.K., Baliu, E.F., Bower, B., Lamsa, M. and Heinsohn, H. (1991) Commercial levels of chymosin production by Aspergillus. Biotechnol. 9, 976–891.
Elagamy, E.I. (2000) Physicochemical, molecular and immunological characterization of camel calf rennet: A comparison with buffalo rennet. J. Dairy Res. 67, 73–81.
Egas, C., Lavoura, N., Resende, R., Brito, R.M.M., Pires, E., Pedroso de Lima, M.C. and Faro, C. (2000) The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage. J. Biol. Chem. 49, 38190–38196.
Faro, C., Verissimo, P., Lin, Y., Tang, J. and Pires, E. (1995) Cardosin A and B, aspartic proteases from the flowers of cardoon. Adv. Exp. Med. Biol. 362, 373–377.
Foltmann, B. (1992) Chymosin: a short review on foetal and neonatal gastric proteases. Scand. J. Clin. Lab. Invest. Suppl. 210, 65–79.
Foltmann, B., Barkholt, P., Kauffman, D. and Wybrandt, G. (1979) The primary structure of calf chymosin. J. Biol. Chem. 254, 8447–8451.
Foltmann, B., Pedersen, V.B., Jacobsen, H., Kauffman, D. and Wybrandt, G. (1977) The complete amino acid sequence of prochymosin. Proc. Natl. Acad. Sci. U S A. 74, 2321–2324.
Fox, P.F. and McSweeney, P.L.H. (1999) Rennets: their role in milk coagulation and cheese ripening. In Microbiology and Biochemistry of Cheese and Fermented Milk. Law, B.A. ed. Blackie Academic and Proffesional, London, pp. 1–49.
Francky, A., Francky, B.M., Strukelj, B., Gruden, K., Ritonja, A., Krizaj, I., Kregar, I., Pain, R. H. and Pungercar, J. (2001) A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin. Eur. J. Biochem. 268, 2362–2368.
Frazao, C. Bento, I., Costa J., Soares, C.M., Verìssimo, P., Faro, C., Pires, E., Cooper, J. and Larrondo, M.A. (1999) Crystal structure of cardosin A, a glycosilated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L. J. Biol. Chem. 274, 27694–27701.
Fujimoto, Z., Fujii, Y., Kaneko, S., Kobayashi, H. and Mizuno, H. (2004) Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin. J. Mol. Biol. 341, 1227–1235.
Gilliland, G.L., Winborne, E.L., Nachman, J. and Wlodawer, A. (1990) The three-dimensional structure of recombinant bovine chymosin at 2.3 Å resolution. Proteins. 8, 82–101.
Groves, M.R., Dhanaraj, V., Badasso, M., Nugent, P., Pitts, J.E., Hoover, D.J. and Blundell, T.L. (1998) A 2.3 Å resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure. Protein Eng. 11, 833–840.
Gustchina, E., Rumsh, L., Ginodman, L., Majer, P. and Andreeva, N. (1996) Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of kappa-casein. FEBS Lett. 379, 60–62.
Harboe, M.K. and Budtz, P. (1999) The production, action and application of rennet and coagulants. In Tecnology of cheese making. Law, B. A. ed. Sheffield Academic Press, Sheffield, pp. 33–65.
Harboe, M.K. and Kristensen, P.B., inventors; Chr. Hansen A/S, assignee. (2000 October 3) Microbially derived enzymes having enhanced milk clotting activity and method producing the same. US Patent 6, 127, 142.
Hiramatsu, R., Aikawa, J., Horinouchi, S. and Beppu, T. (1989) Secretion by yeast of the zymogen form of Mucor rennin, an aspartic proteinase of Mucor pusillus, and its conversion to the mature form. J. Biol. Chem. 264, 16862–16866.
Houen, G., Madsen, M.T., Harlow, K.W., Lonblad, P. and Foltmann, B. (1996) The primary structure and enzymic properties of porcine prochymosin and chymosin. Int. J. Biochem. Cell Biol. 28, 667–675.
Hong, L. and Tang, J. (2004) Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis. Biochem. 43, 4689–4695.
James, M.N.G. (2004) Catalytic pathway of aspartic peptidases. In Handbook of Proteolytic Enzymes. Barrett, A.J., Rawlings, N.D. and Woessner, J.F. eds. Elsevier, London, pp. 12–19.
Jia, Z., Vandonselaar, M., Schneider, P. and Quail, J.W. (1995) Crystallization and preliminary X-ray structure solution of Rhizomucor miehei aspartic proteinase. Acta Crystallogr. D. 51, 243–244.
Kageyama, T. (2002) Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cell Mol. Life Sci. 59, 288–306.
Kappeler, S., Farah, Z., van den Brink, J.M., Rahbeck-Nielsen, H., Budtz, P., inventors; ( 2004 September 16) Method of producing non-bovine chymosin and use hereof. United States Patent Application 20040180410.
Kim, S.Y., Gunasekaran, S. and Olson, N.F. (2004) Combined use of chymosin and protease from Cryphonectria parasitica for control of meltability and firmness of cheddar cheese. J. Dairy Sci. 87, 274–283.
Kobayashi, H., Kusakabe, I. and Murakami, K. (1985) Milk-clotting enzyme from Irpex lacteus as a calf rennet substitute for Cheddar cheese manufacture. Agric. Biol. Chem. 49, 1605–1609.
Marciniszyn, J. Jr., Hartsuck, J.A. and Tang, J. (1976) Mode of inhibition of acid proteases by pepstatin. J. Biol. Chem. 251, 7088–7094.
Mohanty, A.K., Mukhopadhyay, U.K., Grover, S. and Batish, V.K. (1999) Bovine chymosin: Production by rDNA technology and application in cheese manufacture. Biotechnol. Adv. 17, 205–217.
Mohanty, A.K., Mukhopadhyay, U.K., Kaushik, J.K., Grover, S. and Batish, V.K. (2003) Isolation, purification and characterization of chymosin from riverine buffalo (Bubalos bubalis). J. Dairy Res. 70, 37–43.
Newman, M., Safro, M., Frazao, C., Khan, G., Zdanov, A., Tickle, I.J., Blundell, T.L. and Andreeva, sN. (1991) X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 Å resolution of bovine chymosin. J. Mol. Biol. 221, 1295–1309.
Newman, M., Watson, F., Roychowdhury, P., Jones, H., Badasso, M., Cleasby, A., Wood, S.P., Tickle, I.J. and Blundell, T.L. (1993) X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus. J. Mol. Biol. 230, 260–283.
Park, Y.N., Aikawa, J., Nishiyama, M., Horinouchi, S. and Beppu, T. (1996) Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusillus pepsin. Replacement of tyrosine 75 on the flap by asparagines enhances catalytic efficiency. Protein Eng. 9, 869–875.
Pedersen, V.B., Christensen, K.A. and Foltmann, B. (1979) Investigations on the activation of bovine prochymosin. Eur. J. Biochem. 94, 573–80.
Pungercar, J., Strukelj, B., Gubensek, F., Turk, V. and Kregar, I. (1990) Complete primary structure of lamb preprochymosin deduced from cDNA . Nucleic Acids Res. 18, 4602.
Ramalho-Santos, M., Pissarra, J.,Verìssimo, P., Pereira, S., Salema, R., Pires, E. and Faro, C.J. (1997) Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L. Planta. 203, 204–212.
Ramalho-Santos, M., Verìssimo, P., Cortes, L., Samyn, B. Van Beeumen, J., Pires, E. and Faro, C. (1998) Identification and proteolytic processing of procardosin A. Eur. J. Biochem. 255, 133–138.
Rawlings, N.D., Tolle, D.P. and Barret, A.J. (2004) MEROPS: The peptidase database. Nucleic Acid Res. 32 Database issue, D160-D164. http://www.merops.sanger.ac.uk/
Rickert, W.S. and McBride-Warren, P.A. (1974) Structural and functional determinants of Mucor miehei protease. IV. Nitration and spectrophotometric titration of tyrosine residues. Biochim. Biophys. Acta. 371, 368–378.
Rogelj, I., Perko, B., Francky, A., Penca, V. and Pungercar, J. (2001) Recombinant lamb chymosin as an alternative coagulating enzyme in cheese production. J. Dairy Sci. 84, 1020–1026.
Roserio, L.B., Barbosa, M., Ames, J.M. and Wilbey R.A. (2003) Cheesemaking with vegetable coagulants-the use of Cynara L. for the production of ovine milk cheeses. Int. J. Dairy Tech. 56, 76–85.
Sidrach, L., Garcìa-Cànovas, F., Tudela, J. and Rodrìguez-Lòpez, J. N. (2004) Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A. Phytochem. 66, 41–49.
Simöes, I. and Faro, C. (2004) Structure and function of plant aspartic proteinases. Eur. J. Biochem. 271, 2067–2075.
Soares Pais, M.S., Calixto, F.C. and Planta, R.J. inventors; Instituto de Ciencia Aplicada e Technologia, assignee. (2000 December 14) Production by yeast of aspartic proteinases from plant origin. International Patent WO 00/75283 A1.
Tang, J. (2004) Pepsin A. In Handbook of Proteolytic Enzymes. Barrett, A.J., Rawlings, N.D. and Woessner, J.F. eds. Elsevier, London, pp. 19–28.
Tonouchi, N., Shoun, H., Uozumi, T. and Beppu, T. (1986) Cloning and sequencing of a gene for Mucor rennin, an aspartate protease from Mucor pusillus. Nucleic Acids Res. 14, 7557–7568.
Vega-Hernàndez, M.C., Gòmez-Coello, A., Villar, J. and Claverie-Martìn, F. (2004) Molecular cloning and expression in yeast of caprine prochymosin. J. Biotechnol. 114, 69–79.
Vieira, M., Pissarr, J., Verìssimo, P., Castanheira, P., Costa, Y., Pires, E. and Faro, C. (2001) Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculusL. Plant Mol. Biol. 45, 529–539.
White, P.C., Cordeiro, M.C., Arnold, D., Brodelius, P. and Kay, J. (1999) Processing, activity, and inhibition of recombinant cyprosin, an aspartic proteinase from cardoon (Cynara cardunculus). J. Biol. Chem. 274, 16685–16693.
Yamashita, T., Higashi, S., Higashi, T., Machida, H., Iwasaki, S., Nishiyama, M. and Beppu, T. (1994) Mutation of a fungal aspartic proteinase, Mucor pusillus rennin, to decrease thermostability for use as a milk coagulant. J Biotechnol. 32, 17–28.
Yang, J. and Quail, J.W. (1999) Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 Å resolution. Acta Crystallogr. D. Biol. Crystallogr. 55, 625–630.
Yang, J., Teplyakov, A. and Quail, J.W. (1997) Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15- Å resolution. J. Mol. Biol. 268, 449–459.
Yun, J.J., Kiely, L.J., Kindstedt, P.S. and Barbano, D.M. (1993) Mozzarella cheese: impact of coagulant type on functional properties. J. Dairy Sci. 76, 3657–3663.
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Claverie-MartÌn, F., Vega-Hernàndez, M.C. (2007). Aspartic Proteases Used in Cheese Making. In: Polaina, J., MacCabe, A.P. (eds) Industrial Enzymes. Springer, Dordrecht. https://doi.org/10.1007/1-4020-5377-0_13
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