Endothia parasitica

Endothall [45-73-2] Endothelins Endothia parasitica Endothion [2778-04-3] Endotoxin... 

Fig. 10. The effects of chestnut blight (Endothia parasitica) on a deciduous forest ecosystem (after Day Monk, 1974).

The carboxyl proteases are so called because they have two catalytically essential aspartate residues. They were formerly called acid proteases because most of them are active at low pH. The best-known member of the family is pepsin, which has the distinction of being the first enzyme to be named (in 1825, by T. Schwann). Other members are chymosin (rennin) cathepsin D Rhizopus-pepsin (from Rhizopus chinensis) penicillinopepsin (from Penicillium janthinel-lum) the enzyme from Endothia parasitica and renin, which is involved in the regulation of blood pressure. These constitute a homologous family, and all have an Mr of about 35 000. The aspartyl proteases have been thrown into prominence by the discovery of a retroviral subfamily, including one from HIV that is the target of therapy for AIDS. These are homodimers of subunits of about 100 residues.156,157 All the aspartyl proteases contain the two essential aspartyl residues. Their reaction mechanism is the most obscure of all the proteases, and there are no simple chemical models for guidance. 

This aspartic proteinase [EC 3.4.23.22], from the ascomy-cete Endothia parasitica, catalyzes the hydrolysis of proteins with broad specificity similar to that of pepsin A, with preferential action on substrates containing hydrophobic residues at PI and PI. ... 

Alais, C. and Novak, G. 1968. Study of a microbial coagulating enzyme produced by Endothia parasitica. I. Biochemical properties of Pfizer coagulating enzyme (1) and rheological properties of curds formed in the milk. Lait 48, 393-418. 

Reps, A., Poznanski, S. and Kowalska, W. 1970. Characteristics of milk-coagulating proteases obtained from Byssochlamys fulua and Endothia parasitica. Milchwissenschaft. 25, 146-150. 

Reps, A., Poznanski, S., Rymaszewski, J., Jakubowski, J. and Jarmul, I. 1973. Production of milk-clotting enzymes by Byssochlamys fluva and Endothia parasitica moulds. Roczniki Instytutu Przemyslu Mleczarskiego 15, 73-85. 

Thomasow, J., Mrowetz, G. and Schmanke, E. 1970. Experimental cheesemaking with rennet from Endothia parasitica. Milchwissenschaft 25, 211-217. 

Tam, J.T., Whitaker, J.R. 1972. Rates and extents of hydrolysis of several caseins by pepsin, rennin, Endothia parasitica and Mucor pusillus proteinase. J. Dairy Sci. 55, 1523-1531. 

Rennet, Microbial (Endothia parasitica) Produced as an off white to tan, amorphous powder or as a liquid by controlled fermentation using nonpathogenic strains of Endothia parasitica. The powder is soluble in water (the solution is usually tan to dark brown), but practically insoluble in alcohol, in chloroform, and in ether. Major active principle protease. Typical application used in the manufacture of cheese. 

Rennet protease (1) fourth stomach of ruminant animals (2) Endothia parasitica (3) Rhizomucor miehei (4) Rhizomucor pusillus (Lindt) (5) Bacillus cereus none 3.4.23.1 3.4.23.4 3.4.23.22 3.4.23.23... 

Standard Preparation Use a standard-strength rennet, bovine rennet, microbial rennet (Endothia parasitica), or microbial rennet (Mucor species), as appropriate for the preparation to be assayed. Such standards, which are available from commercial coagulant manufacturers, should be of known activity. Dilute the standard-strength material 1 to 200 with water, and mix. Equilibrate to 300 before use, and prepare no more than 2 h before use. 

Rennet, Microbial (nonpathogenic strain of Bacillus cereus), 21 Rennet, Microbial (Endothia parasitica), 21... 

S3)21 Rennet, Microbial (Endothia parasitica), 132, 788, (S3)21 Rennet, Microbial (Rhizomucor (Mucor) sp.), 132, (S3)21 Rennet, Microbial (nonpathogenic strain of Bacillus cereus), 132,... 

Endothia parasitica acid protease Rhodotorida glutinis acid protease... 

Although the general proteolytic activities of various milk clotting enzymes may vary, their milk clotting activities are apparently predicated on the same specific cleavage of the Phe-Met bond in -casein. Apparently rennin, pepsin, chymotrypsin, a microbial protease, proteases from Endo-thia parasitica, Mucor pusillus, and Mucor miehei exert the same type of activity on -casein (2, 169). Enzymes that are currently used commercially for cheesemaking in the United States include rennin, rennin-pepsin mixtures, and microbial proteases from Endothia parasitica, Mucor pusiUus, and Mucor miehei. 

The proteases currently used as coagulants in the cheese industry are known to proteolyze the various casein components. Rennin, porcine pepsin, and proteases from Endothia parasitica, Mucor miehei, and Mucor pusillus readily attack 8-> / -, and K-caseins (195, 199). 

---