Comparative Study of Proteolytic Activities of Some Commercial Milk Clotting Enzymes on Bovine Skim Milk

2002 ◽  
Vol 44 (6) ◽  
pp. 801-808 ◽  
Author(s):  
Yoko Takyu ◽  
Taro Asamura ◽  
Ayako Okamoto ◽  
Hiroshi Maeda ◽  
Michio Takeuchi ◽  
...  

Abstract Aspergillus oryzae RIB40 has 11 aspartic endopeptidase genes. We searched for milk-clotting enzymes based on the homology of the deduced amino acid sequence with chymosins. As a result, we identified a milk-clotting enzyme in A. oryzae. We expected other Aspergillus species to have a homologous enzyme with milk-clotting activity, and we found the most homologous aspartic endopeptidase from A. luchuensis had milk-clotting activity. Surprisingly, two enzymes were considered as vacuole enzymes according to a study on A. niger proteases. The two enzymes from A. oryzae and A. luchuensis cleaved a peptide between the 105Phe-106Met bond in κ-casein, similar to chymosin. Although both enzymes showed proteolytic activity using casein as a substrate, the optimum pH values for milk-clotting and proteolytic activities were different. Furthermore, the substrate specificities were highly restricted. Therefore, we expected that the Japanese traditional fermentation agent, koji, could be used as an enzyme source for cheese production.


1987 ◽  
Vol 54 (2) ◽  
pp. 315-320 ◽  
Author(s):  
Pascaline Garnot ◽  
Daniel Molle ◽  
Michel Piot

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.


2021 ◽  
Vol 9 (3) ◽  
pp. 47
Author(s):  
Ibidjokè Rachidatou Bankole ◽  
Seid Ali Mahamat ◽  
Mouaïmine Mazou ◽  
Sênan Christa Marie Josephine Lokossou ◽  
Fidèle Paul Tchobo

2017 ◽  
Vol 21 (1) ◽  
pp. 9 ◽  
Author(s):  
Wendry Setiyadi Putranto ◽  
Kusmajadi Suradi ◽  
Hartati Chairunnisa ◽  
Apon Zaenal Mustopa ◽  
Puspo Edi Giriwono ◽  
...  

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.  


2000 ◽  
Vol 19 (1-6) ◽  
pp. 49-54 ◽  
Author(s):  
A. Reps ◽  
K. Wiśniewska ◽  
F. Dajnowiec ◽  
M. Iwańczak

2012 ◽  
Vol 21 (1) ◽  
pp. 53-61 ◽  
Author(s):  
Mihir Lal Saha ◽  
K. J. M. Hashina Begum ◽  
Mahbubar Rahman Khan ◽  
Donald James Gomes

Samples collected from different stages of the tannery processing were found to be alkaline. A good number of bacteria were found to be associated with the different stages of leather processing. The aerobic heterotrophic bacterial count ranged in between 11.9 × 106 and 46.7 × 106. The highest count was observed in the soaking stage and the minimum was found with the bating stage. Among 40 isolates, 31 showed positive proteolytic activities on different protein based media. Identified organisms were Bacillus subtilis (9), B. licheniformis (6), B. alcalophilus (2), B. badius (2), B. cereus (2), B. circulans (2), B. pumilus (2), B. alvei (1), B. brevis (1), B. coagulans (1), B. megaterium (1), B. polymyxa (1) and Micrococcus varians (1). Proteolytic activity was measured as zone ratio on skim milk agar which was found to be in between 1.5 and 5.8. Higher zone ratio was observed in B. subtilis (TS/1/E), B. pumilus (TS/1/S1/A3 and TD/S2/C3), B. licheniformis (TS/1/Q) and B.  badius (TD/21-D). The alkaline protease production by the nine selected isolates ranged in between 7.1 and 119.3 U/ml. Two isolates of B. pumilus (TS/1/S1/A3 and TD/S2/C3) were found to be good alkaline protease producers (119.3 and 94.8 U/ml) among the tested organisms. Biotechnologically these two isolates or their enzymes could be utilized in the tannery industry.   Key words: Bacteria, tannery, effluent, alkaline protease   D. O. I. 10.3329/ptcb.v21i1.9563   Plant Tissue Cult. & Biotech. 21(1): 53-61, 2011 (June)


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