Results 1 to 10 of about 6,179,746 (234)

Obtaining of Recombinant Camel Chymosin and Testing Its Milk-Clotting Activity on Cow’s, Goat’s, Ewes’, Camel’s and Mare’s Milk [PDF]

open access: yesBiology, 2022
In the cheese-making industry, commonly chymosin is used as the main milk-clotting enzyme. Bactrian camel (Camelus bactrianus) chymosin (BacChym) has a milk-clotting activity higher than that of calf chymosin for cow’s, goat’s, ewes’, mare’s and camel’s ...
Zhiger Akishev   +8 more
doaj   +3 more sources

High Milk-Clotting Activity Expressed by the Newly Isolated Paenibacillus spp. Strain BD3526 [PDF]

open access: yesMolecules, 2016
Paenibacillus spp. BD3526, a bacterium exhibiting a protein hydrolysis circle surrounded with an obvious precipitation zone on skim milk agar, was isolated from raw yak (Bos grunniens) milk collected in Tibet, China.
Feng Hang   +8 more
doaj   +4 more sources

Plant Milk-Clotting Enzymes for Cheesemaking

open access: yesFoods, 2022
The reduced availability and the increasing prices of calf rennet, coupled to the growing global demand of cheese has led, worldwide, to explore alternative clotting enzymes, capable to replace traditional rennet, during the cheesemaking.
Fabrizio Domenico Nicosia   +4 more
doaj   +4 more sources

PROTEOLYTIC ACTIVITY OF MILK-CLOTTING ENZYMES OF DIFFERENT ORIGIN [PDF]

open access: yesПищевые системы, 2022
The ratio of the milk-clotting activity (MCA) and proteolytic activity (PA) was compared for milk-clotting enzyme preparations (MEP) based on recombinant chymosin, chymosin of animal origin and microbial origin.
D. S. Myagkonosov   +3 more
doaj   +2 more sources

Comparative biochemical properties of recombinant goat and calf chymosins and their implications in dairy processing [PDF]

open access: yesScientific Reports
The nutritional and functional properties of goat milk are well-established. However, the use of camel and calf-derived chymosins during cheese making from goat milk results in relatively low productivity.
Zhiger Akishev   +3 more
doaj   +2 more sources

Cell immobilization for enhanced milk clotting enzyme production from Bacillus amyloliquefacien and cheese quality [PDF]

open access: yesMicrobial Cell Factories
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.
Eman A. Karam   +4 more
doaj   +2 more sources

A new milk-clotting enzyme from noni seeds (Morinda citrifolia L) [PDF]

open access: yesHoehnea, 2022
Proteases are a group of enzymes that catalyze several essential reactions. They are found in all living organisms and in plants has received more attention because of their potential involvement in various industrial processes.
Julyanne Dantas de Oliveira   +1 more
doaj   +1 more source

STUDIES ON ENZYMATIC AND COAGULATING PROPERTIES OF JIBEN (Solanum dubium) SEED EXTRACTS [PDF]

open access: yesJournal of Food and Dairy Sciences, 2007
Studies were carried out to determine the coagulating properties of Jiben (Solanum dubium) seed extracts.  In this study Jiben seeds were extracted with both water and citrate phosphate buffer.
I. Jideani, M. Abubakar, M. Talib
doaj   +1 more source

Constitutive expression of Camelus bactrianus prochymosin B in Pichia pastoris

open access: yesHeliyon, 2021
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

UTILIZATION OF SALT WHEY FROM EGYPTIAN RAS (CEPHALOTYRE) CHEESE IN MICROBIAL MILK CLOTTING ENZYMES PRODUCTION [PDF]

open access: yesJournal of Food and Dairy Sciences, 2012
Microbial milk-clotting enzymes are valued as calf rennet substitutes in the cheese industry. Mucor pusillus QM 436 was identified to produce the highest milk-clotting activity during screening of 19 fungal strains.
Azza Ismail   +4 more
doaj   +1 more source

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