Heat Stable Enzymes from Thermophiles

Abstract

Alkaline phosphatase is widely used in the military and civilian sectors. Commercially available enzyme from calf intestine is the weak link in many applications, breaking down when exposed to elevated temperatures or after being stored for prolonged periods. An extremely heat stable alkaline phosphatase produced by a thermophilic bacterium had been previously identified. The major deficiency was a low specific activity. Research described in this report focused on increasing the specific activity of the heat stable enzyme. This was successfully accomplished by cloning the alkaline phosphatase gene from the wild type into E. coli. One 40-kd cloned product was purified to near homogeneity by nickel affinity chromatography of the N-terminal histidine tagged protein. Purified, cloned alkaline phosphatase exhibited good activity and was thermally stable.

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Document Details

Document Type
Technical Report
Publication Date
Feb 01, 1998
Accession Number
ADA342616

Entities

People

  • Fred Albert
  • Joan Combia
  • Karen Budwill
  • Kenneth Runnion
  • Michael Williamson

Organizations

  • Edgewood Chemical Biological Center

Tags

DTIC Thesaurus Topics

  • Alcohols
  • Amino Acids
  • Calcium Compounds
  • Capillary Electrophoresis
  • Chemical Reaction Properties
  • Chemical Reactions
  • Chemical Warfare Agents
  • Chemistry
  • Chromatography
  • Fungi
  • Heavy Metals
  • Histidine
  • Magnesium Compounds
  • Polymerase Chain Reaction
  • Protein Sequence Analysis
  • Sequence Analysis
  • Sodium Compounds

Fields of Study

  • Biology

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