Results 21 to 30 of about 3,188 (202)
Proteolytic and Textural Parameters of Oil-Ripened Semi-Hard Goat Cheese. [PDF]
ABSTRACT The proteolytic and textural properties of semi‐hard goat cheese ripened in a 50:50 mixture of extra virgin olive oil and refined sunflower oil were investigated. Five batches were divided into three groups: group 1 (control; 60 days air‐ripened), group 2 (10 days air and 50 days oil‐ripened), and group 3 (20 days air and 40 days oil‐ripened).
Levak S +6 more
europepmc +2 more sources
The effect of the type (bovine chymosin (Chy-max Extra), camel chymosin (Chy-max M), and modified camel chymosin (Chy-max Supreme)) and applied dose (1500, 2500, or 3500 IMCU/100 kg of milk) of milk-clotting enzyme (MCE) on the proteolysis degree ...
D. S. Myagkonosov +3 more
doaj +1 more source
Cloning and Expression of Yak Active Chymosin in [PDF]
Rennet, a complex of enzymes found in the stomachs of ruminants, is an important component for cheese production. In our study, we described that yak chymosin gene recombinant Pichia pastoris strain could serve as a novel source for rennet production ...
Fan Luo +4 more
doaj +1 more source
The milk-clotting enzyme chymosin is a member of the group of aspartate proteinases. Chymosin is the main component of rennet traditionally obtained from the stomachs of dairy calves and widely used to coagulate milk in the production of various types of
S. V. Belenkaya +4 more
doaj +1 more source
Constitutive expression of Camelus bactrianus prochymosin B in Pichia pastoris
Camel chymosin can be efficiently employed to produce cheese. Traditionally the rennet enzyme produced by the glands of the fourth stomach of ruminant animals (abomassum) is used in cheese making.
Zhiger Akishev +5 more
doaj +1 more source
Can Recombinant Tree Shrew (Tupaia belangeri chinensis) Chymosin Coagulate Cow (Bos taurus) Milk?
Genetically engineered chymosin from the tree shrew ( Tupaia belangeri chinensis ) has been obtained and partially characterized for the first time. The target enzyme was produced in Escherichia coli , strain BL21(DE3).
D. Balabova +9 more
semanticscholar +1 more source
Comparative analysis of the degree of hydrolysis and antioxidant activity of milk and whey hydrolysates [PDF]
The degree of hydrolysis and antioxidant activity of protein hydrolysates from fresh cow’s milk and whey obtained by the action of the proteolytic enzymes papain, bromelain and chymosin were compared.
Valchkov Alexandar +4 more
doaj +1 more source
Susceptibility of bovine osteopontin to chymosin [PDF]
Osteopontin (OPN) is an acidic phosphorylated glycoprotein found in many tissues and physiological fluids. Bovine OPN is a mature protein comprising 262 amino acids with a calculated molecular weight of 29 kDa. However, SDS-PAGE analysis reveals that the protein isolated from milk migrates to a molecular mass of 60 kDa (Sørensen & Petersen, 1993 ...
Kumura, Haruto +4 more
openaire +3 more sources
The food enzyme chymosin (EC 3.4.23.4) is produced with the genetically modified Kluyveromyces lactis strain CIN by DSM Food Specialties B.V. The genetic modifications do not give rise to safety concerns.
EFSA Panel on Food Contact Materials, Enzyme and Processing Aids (CEP) +23 more
doaj +1 more source
A novel electrochemical assay for chymosin determination using a label-free peptide as a substrate.
Chymosin is a predominant enzyme in rennet and is used in cheese production because of its excellent milk-clotting activity. Herein, we proposed a facile and label-free electrochemical method for determining chymosin activity based on a peptide-based ...
Can-Peng Li +3 more
semanticscholar +1 more source

