Results 151 to 160 of about 6,179,714 (184)
Some of the next articles are maybe not open access.

Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972
Mucor 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 ...
openaire   +2 more sources

Expression, activation and processing of a novel plant milk-clotting aspartic protease in Pichia pastoris

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
openaire   +2 more sources

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

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
openaire   +1 more source

Screening of some Egyptian plants for milk clotting activity

Al-Azhar Journal of Agricultural Research, 2022
A. G. Amer, M. A. Omar, N. S. Abdrabou
openaire   +1 more source

Milk-clotting and proteolytic activities of rennet, and of bovine pepsin and porcine pepsin

Journal of Dairy Research, 1969
SummaryThe 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 ...
openaire   +1 more source

Microbial rennin with enhanced milk-clotting activity

Trends in Food Science & Technology, 1997
openaire   +1 more source

Caseinolytic and milk-clotting activities from flowers

Food Chemistry, 2012
Thiago Henrique Napoleão   +2 more
exaly  

Home - About - Disclaimer - Privacy