Characterization of extracellular amylase produced by haloalkalophilic strain Kocuria sp. HJ014

Int J Environ Health Res. 2016 Aug;26(4):396-404. doi: 10.1080/09603123.2015.1135310. Epub 2016 Jan 27.

Abstract

The haloalkaliphilic bacterium Kocuria sp. (HJ014) has the ability to produce extracellular amylase. The aim of this study was to purify and characterize this protein. The amylase enzyme with a specific activity of 753,502 U/mg was purified 5.7- fold using Sepharose 4B and Sephacryl S-300 gel filtration columns. The molecular weight of the enzyme was 45,000 Da as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The amylase showed maximum activity at pH 9 and 50°C in the presence of 3.5 M NaCl. The Km was 3.0 mg/ml and Vmax 90.09 U/ml. It was found that extracellular amylase from Kocuria sp. has a high industrial potential.

Keywords: Haloalkaliphilic; enzyme molecular weight; industrial potential; specific activity.

MeSH terms

  • Amylases / chemistry
  • Amylases / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Micrococcaceae / enzymology*
  • Molecular Weight

Substances

  • Amylases