https://doi.org/10.17113/ftb.53.01.15.3824
Production and Characterization of α-Amylase from an Extremely Halophilic Archaeon,
Haloferax sp. HA10
Bhakti Bajpai1, Monika Chaudhary2,3 and Jyoti Saxena4*
1Department of Biotechnology, Ashok & Rita Patel Institute of Integrated Study & Research in Biotechnology and Allied Sciences (ARIBAS),
New Vallabh Vidya Nagar 388121, Gujarat, India
2Department of Bioscience and Biotechnology, Banasthali University, Distt. Tonk 304022, Rajasthan, India
3Present address: 13836 Jefferson Park Dr, Apt 9102, Herndon, VA-20171, USA
4Biochemical Engineering Department, B.T. Kumaon Institute of Technology, Dwarahat 263653, Uttarakhand, India
Article history:
Received July 21, 2014
Accepted December 14, 2014
Key words:
halophiles, archaea, α-amylase, Haloferax sp., solar saltern
Summary:
Haloarchaea are found at very high concentrations in salt-conditioned environments, hence produce enzymes which are able to catalyze reactions under harsh conditions, typical of many industrial processes. In the present study, culture conditions for extracellular amylase production from Haloarchaea isolated from a solar saltern were optimized and the purifi ed enzyme was characterized. Haloferax sp. HA10 showed maximum amylase production at 3 M NaCl, 37 °C, pH=7 and 1 % starch content. Purified α-amylase was a calcium-dependent enzyme with an estimated molecular mass of about 66 kDa and many industrially useful properties. It was found to be stable in a broad range of pH (from 5 to 9) and NaCl concentrations (from 0.5 to 3.0 M), retaining 48 % activity even at 4 M. The optimal temperature for Haloferax sp. HA10 amylase activity was 55 °C (99 % activity), and 57 % activity was retained at 80 °C, which dropped to 44 % with the increase of temperature to 90 or 100 °C. It was able to sustain various surfactants and detergents. To the best of our knowledge the detergent-stable α-amylases from halophilic archaeon have not been reported yet.
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