STUDIES ON CHARACTERIZATION OF
EXTRACELLULAR ALKALINE PROTEASE FROM
A MUTANT ASPERGILLUS FLAVUS AS2
M. ROJA RANI AND N.N.PRASAD
Abstract
After our previous purificational studies on Alkaline protease from a mutant of, Aspergillus
flavus AS2 Characterisation of the purified enzyme was done from the culture supernatant by
employing various parameters. The optimum pH and temperature for the activity of alkaline protease
was previously found to be 8.5 and 550C and stable in the pH range 7.0- 8.5. The thermo stability
exhibited by protease ranges from 30-500C.Among various protease inhibitors PMSF strongly inhibited
the enzyme activity revealing that the enzyme in the present study is serine alkaline protease. Ca2+
enhancing effect on the activity of the enzyme. High level of hydrolytic activity was shown by casein
and also found that purified alkaline protease digested the human blood clot, coagulated egg white to
soluble form and also dehairing the goat skin after prolonged incubation. The protease showed good
compatibility and stability in the presence of CaCl2 and glycine with detergents. The enzyme retained
20-40% activity with most of the detergents tested even after 3hrs. The supplementation of the enzyme
preparation in detergents completely removed the blood stain of the cloth. The enzyme followed a
typical Michaelis-Menten kinetics and the apparent Km value was found to be 3.2mgmL-1.
Enter your contact information below to receive full paper.
|
Journal Issues |
Vol 22, Issue 4, 2020
Vol 22, Issue 3, 2020
Vol 22, Issue 2, 2020
Vol 22, Issue 1, 2020
Vol 21, Issue 4, 2019
Vol 21, Nov. Suppl. Issue, 2019
Vol 21, Issue 3, 2019
Vol 21, Issue 2, 2019
Vol 21, Issue 1, 2019
Vol 20, Dec. Suppl. No.2, 2018
Vol 20, Issue 4, 2018
Vol 20, Dec. Suppl. Issue, 2018
Vol 20, Oct Suppl. Issue, 2018
Vol 20, Issue 3, 2018
Vol 20, Issue 2, 2018
Vol 20, Issue 1, 2018
Vol 20, Feb. Suppl. Issue, 2018
Vol 19, Issue 4, 2017
Vol 19, Nov. Suppl, Issue 2017
Vol 19, Issue 3, 2017
Vol 19, Issue 2, 2017
Vol 19, Issue 1, 2017
Vol 18, Issue 4, 2016
Vol 18, Issue 3, 2016
Vol 18, Issue 2, 2016
Vol 18, Issue 1, 2016
Vol 17, Issue 4, 2015
Vol 17, Issue 3, 2015
Vol. 17 Special Issue 2015
Vol 17, Issue 2, 2015
Vol 17, Issue 1, 2015
Vol 16, Issue 4, 2014
Vol 16, Issue 3, 2014
Vol 16, Issue 2, 2014
Vol 16, Issue 1, 2014
Vol 15, Issue 4, 2013
Vol 15, Issue 3, 2013
Vol 15, Issue 2, 2013
Vol 15 Issue 1, 2013
Vol 14, Issue 4, 2012
Vol 14, Issue 3, 2012
Vol 14, Issue 2, 2012
Vol.14, Issue 1, 2012
Vol.13, Issue 4, 2011
Vol.13, Issue 3, 2011
Vol.13, Issue 2, 2011
Vol.13, Issue 1, 2011
Vol.12, Issue 4, 2010
Vol.12, Issue 3, 2010
Vol.12, Issue 2, 2010
Vol.12, Issue 1, 2010
Vol 11, Issue 4, 2009
Vol 11, Issue 3, 2009
Vol 11, Issue 2, 2009
Vol 11, Issue 1, 2009
Vol 10, Issue 4, 2008
Vol 10, Issue 3, 2008
Vol 10, Issue 3, 2008
Vol 10, Issue 2, 2008
Vol 10, Issue 1, 2008
Vol 9, Issue 4, 2007
Vol 9, Issue 3, 2007
Vol 9, Issue 2, 2007
Vol 9, Issue 1, 2007
Vol 8, Issue 4, 2006
Vol 8, Issue 3, 2006
Vol 08, Issue 2, 2006
Vol 08, Issue 1, 2006
Vol 7 Issue 4, 2005
Vol 07, Issue 3, 2005
Vol 07, Issue 2, 2005
Vol 6 Issue 4, 2004
Vol 6 Issue 3, 2004
Vol 6 Issue 2, 2004
Vol 6 Issue 1, 2004
Vol 5 Issue 3, 2003
Vol 5 Issue 2, 2003
Vol 04, Issue 4, 2002
Vol 04, Issue 1, 2002
Vol 3 Issue 1-2, 2001
Vol 1 Issue 1-2, 2000
Vol 1 Issue 3-4, 1999
Vol 1 Issue 1-2, 1999
|
|