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About This Item
Biological source:
microbial (Rhizomucor miehei)
Concentration:
≥4% protein (Lowry)
Product Name
Rennet from Mucor miehei, Type II
biological source
microbial (Rhizomucor miehei)
type
Type II
form
powder
concentration
≥4% protein (Lowry)
storage temp.
−20°C
Quality Level
Application
Rennet from Mucor miehei has been used:
- for milk coagulation trials
- to coagulate the untreated milk and patatin treated milk
- to coagulate the defatted samples of mammary secretions
Studies have shown that heat treatment of milk causes an increase in the rennet-induced coagulation times. This time was proportional to the temperature of the heat treatment.
General description
Rennet, an enzyme extract is mainly used in the dairy industry. Chymosin is the main constituent of rennet. In commercial preparation of rennet, other proteases like bovine pepsin is also present in varying concentrations.
Physical form
Powder containing maltodextrin and sodium chloride
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Impact of Physical-Chemical Properties on Milk Coagulation Ability for Some Albanian Breeds of Cow, Sheep and Goat
Hoxha M and Mara V
International journal of language & communication disorders, 1(3), 234-238 (2012)
Robin Dorau et al.
Applied and environmental microbiology, 87(21), e0103521-e0103521 (2021-08-19)
Lactococcus lactis subsp. lactis (referred to here as L. lactis) is a model lactic acid bacterium and one of the main constituents of the mesophilic cheese starter used for producing soft or semihard cheeses. Most dairy L. lactis strains grow
Potato patatin generates short-chain fatty acids from milk fat that contribute to flavour development in cheese ripening
Spelbrink REJ, et al.
Applied Biochemistry and Biotechnology, 176(1), 231-243 (2015)
Microbial production of enzymes used in food applications
Micro Electro Mechanical Systems (MEMS), 2011 IEEE 24th International Conference on. IEEE, 262-287 (2013)
Factors affecting enzyme activity in food processing
Proteins: Structure, Function, and Genetics, 337-365 (2018)
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