Purification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei

Subject Areas : Journal of Physical & Theoretical Chemistry

Sh. Khalil Moghaddam ¹ , M. Khaleghian ² , F. Naderi ³ , M. Azin ⁴ , M. Monajjemi ⁵

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Received: 2015-05-09 Accepted : 2015-05-09 Published : 2008-11-01

Keywords: RhizoMucor miehei, Milk clotting enzyme (MCE), Purification, Langvin, Molecua,

Abstract :

Milk clotting enzyme (M CE) produced by: Rhizomucor miehei was purified and characterized.The enzyme was purified 220.29-fold with specific activity about 14444.2 U/mg protein byultrafiltration, ammonium sulfate fractionation, Sephacryl S-300 chromatography. The maximumenzyme activity was at 65°C.The milk clotting activity was decreased steadily as pH is increased and indicated maximumactivity at pH 5.3.Ferthermore we did some computational methods for understanding the changesin energy.

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Purification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei