Influence of pH, type of enzyme and ultrafiltration on the retention of milk clotting enzymes in Camembert cheese

1987 ◽  
Vol 54 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Pascaline Garnot ◽  
Daniel Molle ◽  
Michel Piot
Keyword(s):  
Skim Milk ◽  
Mucor Miehei ◽  
Milk Clotting ◽  
Camembert Cheese ◽  
Influence Of Ph ◽  
Enzyme Retention

SummaryCamembert cheeses were made with pasteurized skim milk or with ultrafiltered milk concentrated 2-fold, using either rennet or Mucor miehei proteinase as coagulant. Using rennet, the rapid acidification during cheesemaking increased enzyme retention and 55% was retained after 24 h. With the M. miehei proteinase, acidification had no effect and only 17% of it was retained after 24 h. The use of ultrafiltered milk resulted in less rennet being retained in the curd.

A study of proteolysis during Camembert cheese ripening using isoelectric focusing and two-dimensional electrophoresis

1982 ◽  
Vol 49 (3) ◽  
pp. 501-510 ◽  
Author(s):  
Patrick Trieu-Cuot ◽  
Jean-Claude Gripon
Keyword(s):  
Isoelectric Focusing ◽  
Degradation Products ◽  
Insoluble Fraction ◽  
Similar Action ◽  
Cheese Ripening ◽  
Definition Of ◽  
Camembert Cheese ◽  
Influence Of Ph ◽  
Dimensional Electrophoresis

SUMMABYIsoelectric focusing and 2-dimensional electrophoresis were used to study the development of the pH 4·6-insoluble fraction during Camembert cheese ripening. Modifications of this fraction were due mainly to the action of 5 proteinases: rennet (chymosin + bovine pepsin), plasmin and Penicillium caseicolum aspartyl-and metalloproteinases. Rennet was inactive on β-casein, but acted very early on αs1-casein. However, rennet and P. caseicolum aspartyl-proteinase had a very similar action on the latter substrate, which prevented clear definition of the respective actions of these proteinases on αs1-casein after 7 d of ripening. Plasmin action on β-casein was important from 21 and 35 d of ripening at the surface and in the centre of the cheese respectively, suggesting an important influence of pH changes during maturation. The respective activities of the metallo-and aspartyl-proteinases of P. caseicolum were characterized and followed using β-casein degradation products as markers. The metallo-proteinase activity was detectable immediately after the development of the Penicillium (7 d), while that of the aspartyl-proteinase was observed 3 d later. Thereafter, the amount of β-casein degradation peptides resulting from the metalloproteinase decreased while that resulting from the aspartyl-proteinase increased, suggesting a more important role of the latter enzyme.

Enterococcus faecium 1.15 Isolated from Bakasam Showed Milk Clotting Activity

2017 ◽  
Vol 21 (1) ◽  
pp. 9 ◽  
Author(s):  
Wendry Setiyadi Putranto ◽  
Kusmajadi Suradi ◽  
Hartati Chairunnisa ◽  
Apon Zaenal Mustopa ◽  
Puspo Edi Giriwono ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
16S Rrna ◽  
Enterococcus Faecium ◽  
Skim Milk ◽  
Milk Clotting ◽  
Skim Milk Agar ◽  
Modified Method ◽  
Activity Test ◽  
Milk Clotting Activity

The Lactic Acid Bacteria with Milk Clotting Activity (MCA) were isolated from Bakasam, an Indonesian traditional fermented meat. The isolate screening was carried out using modified method of Skim Milk Agar and Milk Clotting Activity Test, and the isolate was then identified using 16S rRNA. We found 4 isolates that showed MCA of 18-20 SU/ml. Identification using 16S rRNA indicated that the isolate ALG.1.15 was 99% (FR3-F primer) and 99% (FR3-R primer) identic with Enterococcus faecium. The isolate potentially produced renin-like protease to subtitute renin from veal.  

Indirect assay of milk clotting activity of Mucor miehei proteinase (Fromase) in combined rennets

1987 ◽  
Vol 54 (3) ◽  
pp. 407-412 ◽  
Author(s):  
Eva Beránková ◽  
Pavel Rauch ◽  
Jan Káš ◽  
Vladimír Hušek ◽  
Eduard Paluska
Keyword(s):  
Blood Serum ◽  
Proteinase Inhibitors ◽  
Residual Activity ◽  
Total Activity ◽  
Mucor Miehei ◽  
Milk Clotting ◽  
The Difference ◽  
Indirect Assay ◽  
Milk Clotting Activity

SummaryMilk clotting activity of Mucor miehei proteinase (commercial name Fromase) was determined in combined rennets as the difference between the total activity of combined rennet and the residual activity after inhibition of Fromase by the purified immunoglobulin fraction of a Fromase antiserum. The proposed method is simple, rapid, and makes possible the use of any arbitrary method for assaying milk clotting activity. The application of the immunoglobulin fraction, instead of the whole antiserum, is necessary owing to the presence of nonspecific proteinase inhibitors in blood serum.

Selective denaturation of milk coagulants in 5 M-urea

1977 ◽  
Vol 44 (2) ◽  
pp. 319-324 ◽  
Author(s):  
D. M. Mulvihill ◽  
P. F. Fox
Keyword(s):  
Quantitative Assay ◽  
Mucor Miehei ◽  
Milk Clotting

SummaryPorcine and bovine pepsins were very stable in 5·0 M-urea at pH 2·0 or 2·5 at 30 °C while chymosin and Mucor miehei and M. pusillus proteases were rapidly denatured under these conditions. These differences may provide the basis of a quantitative assay of the complement of individual milk clotting enzymes in a coagulant and a possible scheme is suggested.

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