PMID: 9429300Jan 16, 1998Paper

Further characterization and kinetic parameter determination of a milk-clotting protease from Mucor bacilliformis

Applied Biochemistry and Biotechnology
G D VeneraM Biscoglio de Jimenez Bonino

Abstract

Further characterization of an aspartyl protease from Mucor bacilliformis with milk-clotting activity was performed. An extinction coefficient, epsilon 278 cm = 1.61 mL/mg/cm, a molecular mass of 35,400 Da and a pI of 5.2 were determined. Proteolytic activity and kinetic parameters were evaluated by using the hexapeptide Leu-Ser-pNO2-Phe-Nle-Ala-Leu-OMe as the substrate. The effect of pH and temperature on peptide cleavage, as well as protease heat stability, was determined. Such properties, taken as a whole, indicate that the M. bacilliformis protease can be considered a potential substitute for bovine chymosin in cheese manufacture.

Citations

Dec 4, 2010·Applied Microbiology and Biotechnology·Sirma YeginCanan Tari
Feb 28, 2004·Bioresource Technology·M T H CavalcantiA L F Porto
Feb 25, 2003·Chemistry and Physics of Lipids·M F Martini, E A Disalvo
Mar 10, 2006·Journal of Biotechnology·Claudia MachalinskiMirtha Biscoglio de Jiménez Bonino
Jul 17, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·H M Fernandez-LahoreO Cascone
Jul 19, 2014·Applied Biochemistry and Biotechnology·Qian SunZheng-Qiang Jiang

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