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Purification and some properties of a thermostable protease ofThermoactinomyces thalpophilus

  • F. J. C. Odibo
  • S. K. C. Obi
Research Papers

Summary

A thermostable protease fromThermoactinomyces thalpophilus was purified to give a single protein band on disc PAGE with a molecular size of 55000 Da. Optimal proteolytic activity of the purified protease was at pH 6.0 and 70°C. The enzyme was maximally stable between pH 5.0 and 8.0 and retained 62% of its original activity at 70°C after 30 min. Temperature stability was not improved in the presence of Ca2+ (1mm). Enzyme activity was inhibited by AG+, Hg2+, Ba2+ and Co2+, partially inhibited byo-phenanthroline but not by diisopropylfluorophosphate (5mm).

Keywords

Enzyme Purification Enzyme Activity Protein Band Proteolytic Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Résumé

Une protéase thermostable deThermoactinomyces thalpophilus a été purifiée jusqu'à donner une bande protéique unique sur un disque PAGE avec un poids moléculaire de 55000 daltons. L'activé protéolytique optimum de la protéase purifiée se situe à pH 6.0 at à 70°C. L'enzyme présente son maximum de stabilité entre pH 5.0 et 8.0 et conserve 62% de son activité originelle après 30 min à 70°C. La stabilité à la température n'est pas améliorée en présence de Ca2+ 1mm. L'activité enzymatique est inhibée par Ag+, Hg2+, Ba2+ et Co2+. Elle est partiellement inhibée par l'o-phénanthroline mais elle n'est pas inhibée par le di-iso-propylfluorophosphate 5mm.

Resumen

Se purificó una proteína termoestable deThermoactinomyces thalpophilus que dió una sola banda proteica al someterla a una electroforesis en columna de poliacrilamida (PAGE) y un tamaño molecular de 55.000 Da. La actividad proteolítica de la proteína purificada era óptima a pH 6.0 y 70°C. El enzima tenía máxima estabilidad entre pH 5.0 y 8.0 y retuvo un 62% de su actividad original despues de 30 min at 70°C. La estabilidad térmica no mejoró en presencia de Ca2+ (1mm). La actividad enzimática fue Inhibida por Ag+

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Copyright information

© Oxford University Press 1988

Authors and Affiliations

  • F. J. C. Odibo
    • 1
  • S. K. C. Obi
    • 1
  1. 1.Department of MicrobiologyUniversity of NigeriaNsukkaNigeria

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