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).
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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Odibo, F.J.C., Obi, S.K.C. Purification and some properties of a thermostable protease ofThermoactinomyces thalpophilus . Mircen Journal 4, 327–332 (1988). https://doi.org/10.1007/BF01096137
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DOI: https://doi.org/10.1007/BF01096137