Results 1 to 10 of about 3,718 (214)
Production of microbial rennin
Biotechnology Letters, 1988 Fungal strains were compared for their ability to produce milk-coagulating enzyme with low non-specific proteinase activity. Rhizomucor miehei VTT-D-82193 (ATCC 16457) was chosen as the best source of microbial rennin. The enzyme produced compared favourably with two commercial coagulant preparations of microbial origin.
Siika-aho, Matti, Bailey, Michael
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Inactivation of Rennin by Dansyl
Nature, 1966RENNIN (EC 3.4.4.3) is a proteolytic enzyme1 that is of considerable industrial importance because of its ability to clot milk. Evidence has been presented that its clotting action on milk depends on the splitting of an ester bond2. If this is so, the active centre of rennin could be expected to be similar to those of other enzymes with esteraso ...
R D, Hill, R R, Laing
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PAPER CHROMATOGRAPHY OF CASEIN AND RENNIN
Canadian Journal of Medical Sciences, 1951 Purified rennins of very high activity were prepared. The amino acid com position of the hydrolyzates of these preparations was studied by paper chromato graphy. Several fractions were obtained from the purified rennins by paper chromatography showing strong enzyme activity which was comparable to the density of their color development with a ...
Kenneth W. McKerns
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The crystallography of calf rennin (chymosin)
Proceedings of the Royal Society of London Series B, Containing Papers of A Biological Character, 1971Abstract The growth of crystals of calf rennin (chymosin, † EC 3.4.4.3) and the control of nucleation to produce crystals of desired size, are described. Only one stable species, orthorhombic rennin I, has been found, but a metastable monoclinic species, rennin II, appeared on one occasion in a solution nearly saturated with glycine ...
C W, Bunn, P C, Moews, M E, Baumber
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Journal of Biological Education, 1987 The substrate specificity, pH, concentration, and temperature relations of rennin can readily be investigated with only inexpensive commercial rennet and basic laboratory ...
John Gill, Terry Saunders
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JAMA: The Journal of the American Medical Association, 1983 To the Editor.— One often hears speakers discussing the renin-angiotensin-aldosterone system who pronounce the wordreninas "wren-in." This is clearly an error. The correct pronunciation ofreninis "ree-nin." The wordrennin, which is correctly pronounced "wren-in," refers to an enzyme found in calves' stomachs that curdles milk and is used to make ...
James F. Burris
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Journal of Dairy Research, 1971
SummaryA method based on salt fractionation, iso-electric precipitation and gel filtration chromatography is described for the purification of the enzyme rennin (E.C. 3.4.4.3).
A V, Castle, J V, Wheelock
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SummaryA method based on salt fractionation, iso-electric precipitation and gel filtration chromatography is described for the purification of the enzyme rennin (E.C. 3.4.4.3).
A V, Castle, J V, Wheelock
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The action of rennin on casein: The effect of modifying functional groups on the rennin
Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965Summaryk-Casein and whole casein when photo-oxidized in the presence of methylene blue lose the ability to clot when treated with rennin. Two effects are involved—first the photo-oxidation alters the k-casein fraction so that the rennin is unable to split off the glycopeptide fragment, and secondly, in whole casein the photo-oxidation interferes with ...
R D, HILL, R R, LAING
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Nature, 1943
NORTHROP1 has shown that crystallization is a useful procedure in the purification of certain enzymes. Crystalline form, however, is not reliable evidence of purity, as pointed out, for example, by Pirie2, but may be considered as confirmatory evidence.
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NORTHROP1 has shown that crystallization is a useful procedure in the purification of certain enzymes. Crystalline form, however, is not reliable evidence of purity, as pointed out, for example, by Pirie2, but may be considered as confirmatory evidence.
openaire +1 more source