Results 231 to 240 of about 13,591 (265)
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Proteolytic activities of some milk clotting enzymes on ovine casein
Food Chemistry, 2000Proteolytic activity of some milk clotting enzymes (calf and lamb rennets, bovine chymosin and pepsin, and proteases from Rhizomucor miehei and Cryphonectria parasitica) on ovine whole casein was determined by urea-PAGE and RP-HPLC. Microbial enzymes were more proteolytic than animal enzymes when acting on ovine whole casein.
Antonio J. Trujillo +3 more
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Production of highly active fungal milk-clotting enzyme by solid-state fermentation
Preparative Biochemistry & Biotechnology, 2019Cheese production is projected to reach 20 million metric tons by 2020, of which 33% is being produced using calf rennet (EC 3.4.23.4). There is shortage of calf rennet, and use of plant and microbial rennets, hydrolyze milk proteins non-specifically resulting in low curd yields.
Cirium V. Chinmayee +3 more
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Milk-clotting activity of Withania coagulans hairy root extracts
Proceedings of Universities. Applied Chemistry and BiotechnologyThis article presents data on the effect of fruit and hairy root extracts of Withania coagulans Dunal on the process of milk coagulation with a view to its potential application in cheese making. Cheese curd can be obtained by the action of milk-clotting enzymes on the protein fraction of milk.
E. V. Mikhaylova +2 more
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Journal of Biotechnology, 2018
Galium verum, also known as Lady's Bedstraw or Cheese Rennet, is an herbaceous perennial plant traditionally used in cheese-making. We used RACE PCR to isolate novel enzymes from Galium verum with the ability to clot milk. This approach generated two cDNA sequences (named preprogaline A and B) encoding proteins displaying the typical plant aspartic ...
Lucía, Feijoo-Siota +3 more
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Galium verum, also known as Lady's Bedstraw or Cheese Rennet, is an herbaceous perennial plant traditionally used in cheese-making. We used RACE PCR to isolate novel enzymes from Galium verum with the ability to clot milk. This approach generated two cDNA sequences (named preprogaline A and B) encoding proteins displaying the typical plant aspartic ...
Lucía, Feijoo-Siota +3 more
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Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972Mucor miehei produces a protease which is used to replace calf rennet in the cheese industry. Incubation of the enzyme with synthetic substrates indicates that it will hydrolyze peptide bonds having an aromatic amino acid as carboxyl donor. The peptide, carbobenzoxyphenylalanylmethionyl methyl ester containing the bond involved in the milk clotting ...
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Journal of Animal Science and Technology, 2002
Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH
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Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH
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Screening of some Egyptian plants for milk clotting activity
Al-Azhar Journal of Agricultural Research, 2022A. G. Amer, M. A. Omar, N. S. Abdrabou
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Milk-clotting and proteolytic activities of rennet, and of bovine pepsin and porcine pepsin
Journal of Dairy Research, 1969SummaryThe milk-clotting and proteolytic activities of rennet, bovine pepsin and porcine pepsin were compared. The milk-clotting activity of porcine pepsin was extremely pH-dependent around pH 6·6 and coagulation did not occur above pH 6·68. The clotting activity of bovine pepsin was slightly more dependent on pH than that of rennet but no rapid drop ...
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Microbial rennin with enhanced milk-clotting activity
Trends in Food Science & Technology, 1997openaire +1 more source