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Purification and properties of milk-clotting enzyme from Bacillus licheniformis RT7P1
Author(s):
1. Muhammad Sibtain: Gomal University D.I. Khan ,Pakistan
2. Habib Ur Rahman: Gomal University D.I. Khan ,Pakistan
3. Romana Tabassum: National Institute for Biotechnology and Genetic Engineering Faisalabad,Pakistan
4. Sadaf Javaria: Gomal University D.I. Khan ,Pakistan
5. Malik Muhammad Hashim: Gomal University D.I. Khan ,Pakistan
6. Aarif M. Khan: College of Agriculture University of Sargodha,Pakistan
7. Alin Zaman: Gomal University D.I. Khan ,Pakistan
8. Adnan Amin: Gomal University D.I. Khan ,Pakistan
Abstract:
Milk-clotting enzyme production by Bacillus licheniformis RT7P1 was used to study proteolytic and milk-clotting activities of the enzyme using increasing concentrations of skim milk in Basal salt medium by submerged fermentation. The proteolytic and milk-clotting activities were obtained after 120 hours of fermentation with 100% composition of skim milk to the medium. Purified milk-clotting enzyme was obtained by ammonium sulphate precipitation followed by dialysis, DEAE-Cellulose A-50 column and Sephadex G-250 Gel filtration chromatography with 1.25 purification fold and a specific activity of 2.45 U/mg. The optimum proteolytic and milk-clotting activities were at pH 10 and at temperature of 50°C. The metallic ions SrCl2, MnSO4, MnCl2, KCl, NiCl2, FeSO4, increased the PA and MCA of enzyme with increasing concentrations upto 15mM, while MgCl2 increase the activity with 5 mM while decreased the activity when used in higher concentrations. The proteolytic and milk-clotting activities of the enzyme were inhibited by SDS and EDTA. CaCl2 with increasing concentrations from 0.001 to 0.004 mM concentrations increased the milk-clotting activity of the enzyme.
Page(s): 103-103
DOI: DOI not available
Published: Journal: Abstract Book on International Conference on Life Sciences (ICLS-23) 11-12 May 22-23, Volume: 0, Issue: 0, Year: 2023
Keywords:
Bacillus licheniformis
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