Results 141 to 150 of about 200 (179)

Milk-Clotting Enzymes and Cheese Chemistry

1988
Milk-clotting enzymes, obtained from animal, plant, and microbial sources have been used since antiquity for the manufacture of cheese and other foods. Until recently the calf gastric enzyme chymosin (rennin) in the form of a crude extract, paste or powder was used almost exclusively in commercial cheesemaking.
Rodney J Brown
exaly   +2 more sources

Milk-Clotting Enzymes

2021
The use of milk-clotting enzymes in cheese making is one of the oldest enzymatic applications used by man and dates back at least 8000 years. There are different sources of milk-clotting enzymes (animal, microbial, plant), but the main origin has been an extract of suckling-calf abomasa (rennet).
openaire   +1 more source

Investigations on biochemical properties of milk‐clotting enzymes

Food / Nahrung, 1988
AbstractThe properties of proteolytic enzymes produces from calf maws and from an Ascomycete were studied. Both milk‐clotting proteases have their optimum activity at pH 5.2 and 45 °C. The microbiological rennin has a second maximum activity at pH 3.5 and 55 °C.
I, Braun, H, Kunath
openaire   +2 more sources

Recent advances in milk clotting enzymes

International Journal of Dairy Technology, 2010
Coagulating enzymes are an absolute necessity for the production of ripened cheese varieties. The objective of this review is to summarise and interpret the latest findings for the most important types of enzymes, which are animal rennet, genetically engineered chymosin, coagulants of microbial origin, and plant‐derived clotting enzymes.
MANDY JACOB, DORIS JAROS, HARALD ROHM
openaire   +1 more source

Production of milk-clotting enzymes by basidiomycetes

Folia Microbiologica, 1989
BasidiomycetesPhellinus chrysoloma, Kuehneromyces mutabilis andGanoderma applanatum produce extracellular milk-clotting enzymes. The enzymes are acid proteinases stable at 40°C and within pH 3–5.5. Only the enzyme preparation fromP. chrysoloma exhibits properties comparable with animal chymosin.
F. Nerud, Z. Mišurcová, V. Musílek
openaire   +1 more source

Isoelectric focusing of milk-clotting enzymes

Journal of Dairy Research, 1977
SummaryIsoelectric focusing in thin-layer polyacrylamide gel has been applied successfully to the characterization and identification of calf rennet and its substitutes. The use of acidic pH gradients (pH range 2·5–6) allows the identification of calf and microbial rennets and bovine and pig pepsins.A new, very rapid and sensitive zymogram technique ...
P. G. Righetti, Bruna M. Molinari, G. Molinari   +2 more
openaire   +1 more source

Immunological identification of milk-clotting enzymes

Journal of Dairy Research, 1982
SUMMARYThe 6 most widely used milk-clotting enzymes, i.e. chymosin, bovine and porcine pepsins and proteinases from Mucor miehei, M. pusillus and Endothia parasitica, have been purified and used to prepare rabbit antisera against each of them.
Collin, J.C., Muset de Retta, G., Martin, P.   +2 more
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Immunochemical, chromatographic, and milk-clotting activity measurements for quantification of milk-clotting enzymes in bovine rennets

Journal of Dairy Research, 1976
SummaryMonospecific rabbit antibodies were produced against bovine chymosin (rennin) and bovine pepsin A and used for quantitative measurements of these enzymes by rocket immunoelectrophoresis. Bovine pepsin B was identified and measured quantitatively in tandem crossed immunoelectrophoresis, using a polyspecific antibody preparation ...
G A, Rothe, N H, Axelsen, P, Johnk, B, Foltmann   +3 more
openaire   +2 more sources

Activity and Properties of the Penicillium citrinum Milk-clotting Enzyme

Zentralblatt für Bakteriologie, Parasitenkunde, Infektionskrankheiten und Hygiene. Zweite Naturwissenschaftliche Abteilung: Allgemeine, Landwirtschaftliche und Technische Mikrobiologie, 1974
Summary In the presence of substrate, the milk-clotting enzyme preparation of Penicillium citrinum showed a good stability against heat and p H changes. A linear relationship was observed between the amount of the enzyme and the reciprocal of clotting time. The rate of milk-clotting depended on a certain ratio between the enzyme and the substrate.
A F, Abdel-Fattah, N M, El-Hawwary
openaire   +2 more sources

Production of milk-clotting and proteolytic enzymes by fungi

Agricultural Wastes, 1984
Abstract Production of extracellular and intracellular milk-clotting, caseinase and gelatinase enzymes by 12 fungal cultures was investigated. Production of these enzymes was better in surface than in shaken cultures. The sequence of production of these enzymic activities during incubation differed according to the age and type of the culture.
Abdel-Mohsen S. Ismail, Samy A. El-Aassar, Ahmed F. Abdel-Fattah   +2 more
openaire   +1 more source