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Mucor rennins

Penicillopepsin Aspergillopeptidase A Aspergillus oryzae acid protease Rhizopus-pepsin Mucor rennins... [Pg.148]

Hiramatsu R, Aikawa J, Horinouchi S et al. (1989) Secretion by yeast of the zymogen form of Mucor rennin, an aspattic proteinase of Mucor pusillus, and its conversion to the mature form. The J Biol Chem 264(28) 16862-16866... [Pg.95]

NOTE 16 At least 14 fungal and protozoal proteinases of broad activity are listed under 3.4.23.6. Among these are Takadiastase, Trypsinogen kinase, Aspergillopeptidase, Penicillopepsin, Peptidase A, Mucor rennin. Baker s yeast proteinase A, and carboxyl proteinases from 3 species of Aspergillus, strains of Penicillium, Rhizopus, Endothia, Mucor, Candida, Paecilomyces, Sac--... [Pg.229]

Richardson, G. H., Nelson, J. H., Lubnow, R. E. and Schwarberg, R. L. 1967. Rennin-like enzyme from Mucor pusillus for cheese manufacture. J. Dairy Sci. 50, 1066-1072... [Pg.632]

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. [Pg.438]

The use of other acid proteases as substitutes for rennin in cheese making is determined by whether bitter peptides are formed during ripening of the cheese and by whether initial rapid hydrolysis causes excessive protein losses in the whey. Some of the acid proteases used in cheese making include preparations obtained from the organisms Endo-thia parasitica, Mucor miehei, and Mucor pusillus. Rennin contains the enzyme chy-mosin, and the scarcity of this natural enzyme preparation for cheese making resulted in the use of pepsin for this purpose. Pepsin and chymosin have primary structures that have about 50 percent homology... [Pg.302]

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. [Pg.224]

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). [Pg.232]

Seker, S., Beyenal, H., Ayhan, R, and Tanyolac, A., Production of microbial rennin from Mucor miehei in a continnonsly fed fermenter. Enzyme Microbiol. Technol., 23,469,1998. [Pg.128]

Aspartic proteinases of microbial origin can be classified as pepsin-like or rennin-like enzymes. The latter are able to coagulate milk. The pepsin-like enzymes are produced, for example, by Aspergillus awamori, A. niger, A. oryzae, Penicillium spp, and Trametes sanguinea. The rennin-like enzymes are produced, for example, by Aspergillus usamii and Mucor spp., such as M. pusillus. [Pg.79]


See other pages where Mucor rennins is mentioned: [Pg.163]    [Pg.147]    [Pg.150]    [Pg.152]    [Pg.157]    [Pg.163]    [Pg.147]    [Pg.150]    [Pg.152]    [Pg.157]    [Pg.85]    [Pg.1381]    [Pg.150]    [Pg.67]    [Pg.967]    [Pg.495]   
See also in sourсe #XX -- [ Pg.148 ]




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