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Preparation and some chemical characteristics of milk-clotting protease from Bacillus mesentericus 76
International Journal of Peptide and Protein Research
|January 1, 1981
Abstract:
Pure milk-clotting protease (MCP-76) is isolated by isotachophoresis at pH 5.0. The native molecule has only one protein chain. It is a metaloenzyme containing zinc. The pure MCP-76 has a molecular weight of 33 000 (+/- 1500) and by diphenyl-indenonyl-isothiocyanate method showed arginine as N-terminal amino acid.
Insights
Researchers isolated pure milk-clotting protease (MCP-76), a zinc-containing metalloenzyme. This study characterized its molecular weight and N-terminal amino acid, arginine.
Area of Science:
- Enzymology
- Protein Chemistry
- Biochemistry
Background:
- Milk-clotting proteases are crucial in dairy processing.
- Characterization of these enzymes aids in understanding their function and application.
- Metalloenzymes represent a significant class of enzymes with diverse biological roles.
Purpose of the Study:
- To isolate and purify milk-clotting protease (MCP-76).
- To characterize the biochemical properties of the purified MCP-76.
- To identify the N-terminal amino acid of MCP-76.
Main Methods:
- Isotachophoresis at pH 5.0 for protein isolation.
- Molecular weight determination.
- Diphenyl-indenonyl-isothiocyanate method for N-terminal analysis.
Main Results:
- Pure milk-clotting protease (MCP-76) was successfully isolated.
- The enzyme is a monomeric metalloenzyme containing zinc.
- The molecular weight was determined to be 33,000 ± 1500 Da.
- Arginine was identified as the N-terminal amino acid.
Conclusions:
- MCP-76 is a well-defined, monomeric metalloenzyme.
- The characterization provides fundamental data for MCP-76.
- Understanding MCP-76's properties can inform its use in food science and biotechnology.