Accession Number : ADA342616


Title :   Heat Stable Enzymes from Thermophiles


Descriptive Note : Final rept. Mar 95-Mar 97


Corporate Author : EDGEWOOD RESEARCH DEVELOPMENT AND ENGINEERING CENTER ABERDEEN PROVING GROUNDMD


Personal Author(s) : Williamson, Michael ; Combia, Joan ; Albert, Fred ; Runnion, Kenneth ; Budwill, Karen


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a342616.pdf


Report Date : FEB 1998


Pagination or Media Count : 76


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.


Descriptors :   *HIGH TEMPERATURE , *ENZYMES , *THERMAL STABILITY , *ESCHERICHIA COLI , *THERMOPHILIC FUNGUS , EXPOSURE(GENERAL) , BACTERIA , GENES , CLONES , NICKEL , CIVILIAN POPULATION , GENETIC ENGINEERING , WILDLIFE , CHROMATOGRAPHY , HOMOGENEITY , ALKALINITY , PHOSPHATASES.


Subject Categories : MEDICINE AND MEDICAL RESEARCH
      STRESS PHYSIOLOGY
      MICROBIOLOGY


Distribution Statement : APPROVED FOR PUBLIC RELEASE