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- Title
Purification and characterization of ß-galactosidase from Aspergillus fumigatus PCSIR-2013.
- Authors
Bano, Saeeda; Iqbal, Samina; Siddiqui, Kauser; Abbasi, Kanwal
- Abstract
Extra cellular β-galactosidase enzyme was purified and characterized from Aspergillus fumigatus PCSIR-2013. Estimated molecular mass of the enzyme was approximately 95 kDa. by native polyacrylamide gel electrophoresis. Initially, different fermentation parameters were optimized for maximum production of β-galactosidase. The kinetic study of the partially purified enzyme exhibited that it remained active in broad range of temperature from 25°C to 70°C with an optimum of 60°C. The Km and Vmax were calculated as 9.95mmol/l and 51.78 U/ml/min, respectively. The optimum pH was 5.0, when reaction mixture was incubated for 30 min. The enzyme was very stable in the presence of different metal ions, although Na+ (16%) stimulates the activity at 10mM concentration. In contrast, Ba+2 and Hg+2 have negative effect on enzyme activity and activity decreased to 54% and 19%, respectively. Thermo stability study was revealed that the enzyme retained 72% of its activity at 50°C. Whereas, when enzyme was incubated at 60°C for 120 min, its residual activity was decreased to 42.0%. However, the enzyme was completely inactivated at 80°C after 120 min of pre-incubation. Among different surfactant which incorporated with enzyme, Tween 20 and Triton X-100 both have stimulatory effect and activity increased to 29% and 17%, respectively.
- Subjects
ASPERGILLUS fumigatus; POLYACRYLAMIDE gel electrophoresis; GALACTOSIDASES; MOLECULAR weights; TRITON X-100
- Publication
Pakistan Journal of Pharmaceutical Sciences, 2021, Vol 34, Issue 4, p1333
- ISSN
1011-601X
- Publication type
Article
- DOI
10.36721/PJPS.2021.34.4.REG.1333-1340.1