Purification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei
الموضوعات : Journal of Physical & Theoretical Chemistry
Sh. Khalil Moghaddam
1
(-)
M. Khaleghian
2
(-)
F. Naderi
3
(-)
M. Azin
4
(-)
M. Monajjemi
5
(-)
الکلمات المفتاحية: RhizoMucor miehei, Milk clotting enzyme (MCE), Purification, Langvin, Molecua,
ملخص المقالة :
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.
