The ratio of milk-clotting activity to proteolytic activity (MC/PA) was used as an index to determine the quality of milk-clotting enzyme. Solid-state fermentation on wheat bran for 5 days at room temperature gave optimal production for enzyme by Rhizomucor miehei and R. pusillus. A ratio of wheat bran to moisture of 1:0.6 (w/v) gave best results. Adding skim milk powder to the media of R. miehei did not improve the MC/PA ratio but 4% (w/w) of the powder did improve the ratio with R. pusillus. Co-cultivation of R. miehei with R. pusillus did not change the MC/PA ratio.
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http://dx.doi.org/10.1007/BF00367659 | DOI Listing |
Microb Cell Fact
October 2024
Chemistry of Natural and Microbial Products Department, Pharmaceutical Industries and Drug Research Institute, National Research Centre, Dokki, Cairo, 12622, Egypt.
Background: Milk clotting enzymes, essential for milk coagulation in cheese production, are obtained from the stomach of young ruminants, an expensive and limited source. This study was accomplished by finding a suitable alternative. Bacterial isolates recovered from honey were screened for milk clotting enzyme activity.
View Article and Find Full Text PDFInt J Biol Macromol
October 2024
Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil. Electronic address:
Thermolysin (TLN) is a microbial highly-priced thermostable metallo-endoprotease with complementary substrate specificity to those of proteases widely used in science and industry for protein digestion and milk-clotting. This study is the first to immobilize TLN on aminated superparamagnetic nanoparticles (FeO@silica-NH) aiming for higher stability, recoverability, reusability, and applicability in proteolysis and as a microbial rennet-like milk-clotting enzyme. The nanobiocatalyst developed (FeO@silica-TLN) displays hydrolytic activity on a synthetic TLN substrate and, apparently, was fully recovered from reaction media by magnetic decantation.
View Article and Find Full Text PDFFoods
October 2023
Federal Altai Scientific Center for Agrobiotechnologies, Siberian Research Institute of Cheese Making, 656910 Barnaul, Russia.
Moose () recombinant chymosin with a milk-clotting activity of 86 AU/mL was synthesized in the expression system. After precipitation with ammonium sulfate and chromatographic purification, a sample of genetically engineered moose chymosin with a specific milk-clotting activity of 15,768 AU/mg was obtained, which was used for extensive biochemical characterization of the enzyme. The threshold of the thermal stability of moose chymosin was 55 °C; its complete inactivation occurred after heating at 60 °C.
View Article and Find Full Text PDFFood Res Int
October 2023
School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China. Electronic address:
Milk-clotting enzyme (MCE) is a crucial active agent in cheese making. It is necessary to find traditional MCE substitutes due to the limited production of traditional MCE (e.g.
View Article and Find Full Text PDFJ Dairy Sci
October 2023
School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China. Electronic address:
Milk-clotting enzyme (MCE) is the essential active agents in dairy processing. The traditional MCE is mainly obtained from animal sources, in which calf rennet is the most widely used in cheese industry. Traditional MCE substitute is becoming necessary due to its limited production and increased cheese consumption.
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