Results 131 to 140 of about 3,188 (202)
Some of the next articles are maybe not open access.
Study of milk coagulation induced by chymosin using atomic force microscopy
Food Bioscience, 2019Caseins (αs1-, αs2, β-, and κ-caseins) form the major protein fraction of milk, irrespective of their origins. They are able to form well-ordered colloidal structures in association with colloidal calcium phosphate, named casein micelles.
Cleverson D T Freitas
exaly +2 more sources
Bioresource Technology
As an important industrial enzyme, chymosin has been widely used in cheese manufacturing. Fermentation with Kluyveromyces lactis has allowed recombinant chymosin production to fit the growing global demand for cheese consumption; yet improvements can be ...
Yanli Zheng +9 more
semanticscholar +1 more source
As an important industrial enzyme, chymosin has been widely used in cheese manufacturing. Fermentation with Kluyveromyces lactis has allowed recombinant chymosin production to fit the growing global demand for cheese consumption; yet improvements can be ...
Yanli Zheng +9 more
semanticscholar +1 more source
Factors influencing the gelation and rennetability of camel milk using camel chymosin
International Dairy Journal, 2016 Yonas Hailu +2 more
exaly +2 more sources
Journal of Dairy Science, 2019 Beyaz peynir, a white brined cheese, was manufactured using different blends of camel chymosin (100, 75, 50, 25, and 0%) with calf chymosin and ripened for 90 d.
P. Gumus, A. A. Hayaloğlu
exaly +2 more sources
Effect of fermentation-produced camel chymosin on quality of Crescenza cheese
International Dairy Journal, 2018Quality properties of Crescenza cheese, a typical Italian soft cheese with a short shelf life, are negatively affected by proteolysis due to residual rennet activity, causing a bitter taste and excessive softening of its structure.
Marcello Alinovi, Germano Mucchetti
exaly +2 more sources
The crystallography of calf rennin (chymosin)
Proceedings of the Royal Society of London. Series B. Biological Sciences, 1971The growth of crystals of calf rennin (chymosin, † EC 3.4.4.3) and the control of nucleation to produce crystals of desired size, are described. Only one stable species, orthorhombic rennin I, has been found, but a metastable monoclinic species, rennin II, appeared on one occasion in a solution nearly saturated with glycine.
C W, Bunn, P C, Moews, M E, Baumber
openaire +2 more sources
Increased production of chymosin by glycosylation
Journal of Biotechnology, 2006Filamentous fungi are well known in the industry as producers of large amounts of extracellular proteins. However, production levels of heterologous proteins are often disappointing low. In this paper it is shown that increasing glycosylation is a powerful strategy for increasing production levels of chymosin in filamentous fungi.
Hans J M, van den Brink +4 more
openaire +2 more sources
Thermal inactivation of chymosin during cheese manufacture
Journal of Dairy Research, 2002The aspartic proteinase, chymosin (EC 3.4.23.4) is the principal milk clotting enzyme used in cheese production and is one of the principal proteolytic agents involved in cheese ripening. Varietal differences in chymosin activity, due to factors such as cheese cooking temperature, fundamentally influence cheese characteristics.
Maurice G, Hayes +3 more
openaire +2 more sources
Large-scale production of yak (Bos grunniens) chymosin A in Pichia pastoris.
Protein Expression and Purification, 2019Milk-clotting enzymes used in the dairy industry can be obtained from different sources such as plants, animals, and microorganisms. Recombinant chymosin is the best alternative for the dairy industry due to the differences in physicochemical properties ...
F. Ersöz, Mehmet Inan
semanticscholar +1 more source