Detergent stable, halotolerant -amylase from bacillus aquimaris vitp4 exhibits reversible unfolding.
Loading...
Date
2011-04
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Halotolerant Bacillus aquimaris VITP4, isolated from Kumta coast (India), was used
to produce extracellular α-amylase. The production was found to be maximal after 24 h of growth at
pH 8.0 and 40 oC. Optimal activity of the purified enzyme was in the pH range of 7.5 – 9.5 at 40 oC.
The enzyme was found to retain more than 60% of the initial activity even at NaCl concentration of
3.5 M, indicating that it is halotolerant. Calcium ion (0.01 mM) and CTAB (10 mM) enhanced the
activity whereas EDTA decreased the enzymatic activity. Thermal inactivation kinetics suggested that
the enzyme exhibits reversible unfolding even at high temperature (till 90 oC) and the t1/2 at 90 oC was
found to be 43.5 min. These results suggests that the α-amylase from Bacillus aquimaris strain VITP4
is halotolerant, metal ion dependent enzyme which is stable in the presence of cationic detergent and
moderate temperature conditions.
Description
Keywords
Bacillus aquimaris VITP4, halotolerant, α-amylase, calcium ion, reversible unfolding, CTAB
Citation
Anupama A, Jayaraman G. Detergent stable, halotolerant -amylase from bacillus aquimaris vitp4 exhibits reversible unfolding. International Journal of Applied Biology and Pharmaceutical Technology. 2011 Apr-June; 2(2): 366-376.