Browsing by Author "Omidiji, O."
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Item Effect of carbon and nitrogen sources on glucoamylase production inLactobacillus brevis(springer, 1996-04-11) Ilori, Matthew O.; Amund, Olukayode O.; Omidiji, O.A strain of Lactobacillus brevis produced extracellular glucoamylase. Induction of the glucoamylase occurred when saccharides such starch, dextrin, maltose, mannitol and sucrose were employed as sole carbon sources. Synthesis of the amylase also occurred when soybean extract and peptone were used as sole nitrogen sources. The organism could be employed as a starter culture for local food fermentation.Item Production of Amylase in a Corn Steep Liquor-Soya Bean Meal Medium by a Strain of Baccillus Stearothermophilus(The faculty press, Cambridge, 1997) Omidiji, O.; Amund, Olukayode O.; Braimoh, A. A.; Ilori, Matthew O.Corn grains (Zea mays, yellow variety) were steeped in water for 10 days and parameters such as pH, protein, amino acids, lipid, soluble starch and reducing sugar content were measured at 2 day intervals in the steep liquor. The pH decreased from 7.0 to 5.4 during the steeping period. The protein content ranged between 1.25 and 11.25 mg/ml; lipid content ranged between 0.3 and 3.2 mg/ml. The soluble starch concentration increased from 212 to 530 mg/ml, and the reducing sugar concentration reduced from 2.54 to 1.13 mg/ml. A fermentation medium was compounded from 2-day old liquor to cultivate an amylolytic strain of Bacillus stearothemophilus. Peak production of amylase occurred at 240 h while the highest cell density occurred at 144 h. Various concentrations of soluble starch (0.5-5%, w/v) and soya bean meal (0.1-0.5 %, v/v) were used in cultivating the organism. The highest amylase activity was recorded with 2 % (w/v) starch, while 0.5 % (v/v) of soya bean meal supported the greatest growth. The medium could be exploited for industrial amylase production.Item Purification and Properties of a Neutral Protease Produced by Lactobaccillus Brevis(Kluwer Academic Publishers, 1990-09-01) Ilori, Matthew O.; Amund, Olukayode O.; Omidiji, O.An extracellular glucose-forming amylase was produced by Lactobacillus brevis isolated from ‘Kagasok tea’. The enzyme was purified 70-fold and had optimal activity at 55 oC and pH 6.5. Its Km value for starch was 0.27 mg ml-1 and its M, was approx. 75,900 Da. The activity of the enzyme was enhanced by Ca2+, Mg2+, Na+ or K+ and inhibited by EDTA, KCN, citric acid and L-cysteine.Item Purification and properties of a neutral protease produced by Lactobacillus brevis(Elsevier, 1990-03-01) Amund, Olukayode O.; Omidiji, O.A proteolytic enzyme was produced by a strain of Lactobacillus brevis isolated from an oriental beverage. The enzyme was extracted and purified 50-fold by gel filtration and ion-exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 35°C and the molecular weight 34,674 Da. Furthermore, the enzyme was stimulated by cations including Ca2+, Mg2+, Na+ and K+ and inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, ascorbic acid and citric acid. The enzyme is probably a neutral metalloprotease.Item Purification and properties of an α-amylase produced by a cassava-fermenting strain of Micrococcus luteus(Springer Netherlands, 1997-10-01) Ilori, Matthew O.; Amund, Olukayode O.; Omidiji, O.An extracellular α-amylase produced by a cassava-fermenting strain of Micrococcus luteus was purified 26-fold by gel filtration and ion-exchange chromatography. The molar mass was estimated to be approximately 56 kDa. The optimum temperature of the enzyme was 30oC, optimum pH 6.0 and optimum substrate concentration was 0.6 % (w/v). Treatment of the enzyme at 70 oC for 10 min resulted in 70 % loss of activity. The activation energy was determined to be 34.8 kj/mol. The activity of the enzyme was enhanced by Mg2+, Ca2+, K+, Na+ and inhibited by EDTA, KCN and citric acid. The enzyme may find some application in local food processing.