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Articles by P.O. Olutiola
Total Records ( 5 ) for P.O. Olutiola
  A.O. Adejuwon and P.O. Olutiola
  Lasidioplodia theobromae grew in a culture medium at 27 °C producing proteins which showed pectin lyase activity. The enzyme was purified by a combination of ammonium sulphate precipitation, dialysis, gel permeation and ion-exchange chromatography. Optimum activity of the enzyme was at 40°C and at pH 8.5. The enzyme was stimulated by concentrations of K+, Na+, Ca++ and Mg++ but inhibited by EDTA and Hg++. When the enzyme was heated at 70 °C, optimum activity had decreased by about 66.6% within 2 min but almost completely lost within 30 min. The enzyme was able to degrade pectin with optimum activity expressed at 18-20 mg mL-1.
  A.O. Adejuwon and P.O. Olutiola
  Penicillium species grew in a synthetic medium with pectin as the sole carbon source producing proteins which expressed alkaline pectin lyase activity. The enzyme was purified by a combination of ammonium sulphate precipitation, dialysis, gel filtration and ion-exchange chromatography. Optimum activity of the enzyme was at 35°C and at pH 80. The enzyme was stimulated by K+, Na+, Ca++ and Mg++ but inhibited by EDTA and Hg++. The enzyme was able to degrade pectin with optimum activity expressed at 16 mg mL‾1.
  A.O. Adejuwon , O.A. Oni and P.O. Olutiola
  Tomato fruits infected with Penicillium funiculosum Thom. produced proteins which showed appreciable polygalacturonase activity within eight days. Uninfected tomato fruits showed only traces of polygalacturonase activity. The enzyme was partially purified by a combination of gel filtration and ion-exchange chromatography. Two components with molecular weight estimates of approximately 223,800 daltons and 89,100 daltons were expressed. Only the components of the lighter peak showed polygalacturonase activity. The enzyme showed optimum activity at pH 4.5 and 40°C. It possessed an apparent Km of 0.05 mg mL-1 for the hydrolysis of pectin. Na+ and CaH ions were stimulatory to the activity of the enzyme. EDTA and Hg++ were inhibitory.
  A.A. Ajayi , A.O. Adejuwon , O.K. Awojobi and P.O. Olutiola
  Within ten days of incubation, freshly ripe tomato fruits (Ibadan local variety) obtained from a local market in Ile-Ife, Osun State, Nigeria had completely deteriorated and proteins which possessed cellulolytic activity were released. The enzyme was partially purified by a combination of ammonium sulphate precipitation, molecular exclusion chromatography and ion-exchange chromatography. The enzyme was stimulated to varying degrees by Ca++, Mg++, Na+ and K+ but was inhibited by ethylene diamine tetraacetic acid, 2, 4-dinitrophenol and mercuric chloride.
  A.O. Adejuwon and P.O. Olutiola
  Tomato fruits infected with Fusarium oxysporum produced proteins which exhibited proteolytic activity. The enzyme was partially purified by molecular exclusion and ion-exchange chromatography. Two components with molecular weight estimates of approximately 112, 000 and 63,100 were expressed. The enzyme exhibited maximum activity at pH 6.0 and 35°C. It possessed an apparent Km of approximately 4.3 mg mL-1 for casein. The enzyme was stimulated by the monovalent cations, Na+ and K+ and by the divalent cations; Mg++ and Ca++ but inhibited by ethylene diamine tetra acetic acid and mercuric chloride.
 
 
 
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