83553
Rennin from Mucor miehei
lyophilized, powder, slightly brown, ~0.1 U/mg
Synonym(s):
Mucorpepsin
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About This Item
biological source
fungus (Mucor miehei)
form
powder
quality
lyophilized
specific activity
~0.1 U/mg
mol wt
Mr ~40000
color
slightly brown
storage temp.
−20°C
Unit Definition
1 U corresponds to the amount of enzyme which liberates 1 μmol folin-positive amino acids and peptides (calculated as tyrosine) per minute at pH 7.5 and 37°C (casein, Cat. No. 22078, as substrate)
Other Notes
Action on a synthetic chromophoric hexapeptide
Sales restrictions may apply
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Certificates of Analysis (COA)
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Hongyan Sun et al.
Biopolymers, 88(2), 141-149 (2007-01-09)
We have successfully developed a protease assay using fluorescence resonance energy transfer based peptide libraries, which allows not only general detection of enzymatic activities, but more importantly substrate fingerprinting of proteases from different classes. The method allows the generation of
Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease.
M Sternberg
Biochimica et biophysica acta, 285(2), 383-392 (1972-12-28)
M Baudys et al.
FEBS letters, 235(1-2), 271-274 (1988-08-01)
The amino acid sequence of Mucor pusillus aspartic proteinase was determined by analysis of fragments obtained from cleavage of the enzyme by CNBr and limited tryptic digestion. The proteinase is a single polypeptide chain protein containing 361 amino acid residues
P Martin et al.
Biochimica et biophysica acta, 612(2), 410-420 (1980-04-11)
The action of two milk-clotting fungal proteases from Mucos pusillus and Mucor miehei and of chymosins A and B on the hexapeptide, Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe, and on kappa-casein were studied. The effects of pH and temperature on the initial rates of hydrolysis
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