4 research outputs found

    Chemical, sensory and microbiological properties of food bars prepared from oil seed flours

    No full text
    Suitable processing technology for the production of nutritious calorie food bars from indigenous oil seeds was studied and developed. Food bars were produced from blends of quantities of peanut cake, soybean flour and sesame seeds as the main base. Other ingredients were sorghum flour as carbohydrate base, while carrot and coconut shreds served as fruit base. These were thoroughly mixed and moistened with honey, and were added to a mixture of boiling caramel and soy lecithin. Sensory attributes of sugar caramel, proximate and chemical composition, metabolizable energy, textural properties and microbiological qualities of the food bars produced were determined. There was no significant difference in the colour and hardness for sugar caramel produced at 150-1800C but the taste was significantly different 180oC. The moisture content of food bars ranged from 4.20-4.43%, protein 18.06-19.62g, fat 21.23-22.56g, crude fibre 4.55-4.98g, ash 2.81-3.53g and carbohydrate 45.11-48.85g, respectively. The average chemical composition of bars (g/100g) showed that 33.80% of protein, 35.99% of carbohydrate, 12.47% of fibre and 20.89% of energy (based on 2200kCal of energy/day) were obtained for an adult woman RDA. The average component energies from protein, fat, carbohydrate contents and added sugar were 16.48%, 42.80%, 46% and 17.41%, respectively. The textural property showed increases directly with increasing sugar level (18-22%). The highest deflection (2.38 ± 0.724mm) was recorded for the bar produced at 20% sugar level, while the least (1.21 ± 0.184mm) was recorded for the bar produced at 18%. Salmonella spp., staphylococcus spp. and fungi were not detected in all the calorie bar samples analyzed.Keywords: Food bar, processing technology, proximate, textural properties, microbiological qualitie

    Characterization of Novel Alkaline Protease producing Bacillus subtilis C3a-FIIRO with Potential for Industrial Application

    Get PDF
    Microbial alkaline protease is one of the dominant industrial enzymes which function in splitting polypeptides chain of protein into monomers of amino acids and peptides. This study aimed to identify alkaline protease produced by Bacillus sp. Soil samples were aseptically collected from dump sites in FIIRO, Lagos state, Nigeria. The samples were serially diluted, and bacteria were isolated using pour plate method. The resulting isolates were screened and morphologically characterized. The isolate with the highest protease production potential was subjected to biochemical characterization using Analytical Profile Index (API) identification kit system and 16S rRNA sequencing. The selected isolate was used to produce alkaline protease by solid state fermentation using rice bran as a substrate. Out of the 18 bacteria isolated, 11 isolates showed alkaline protease production potential. Isolate C3a-FIIRO was selected for its maximal alkaline protease produced as indicated by a 56 mm zone of clearance. Morphological and biochemical characterization revealed isolate C3a-FIIRO as a member of the genus Bacillus. The 16S rRNA gene sequencing confirmed the isolate as Bacillus subtilis C3aFIIRO (MW577298) with closest homology to Bacillus subtilis Y17B. The enzyme activity of 6848.171 U/ml ± 0.11 and protein concentration of 152.13 mg/ml ± 0.003 showed that Bacillus subtilis C3a-FIIRO has potential for sustainable alkaline protease production

    Production and Partial Purification of Amylase By Aspergillus niger Isolated from Cassava Peel

    No full text
    Aspergillus niger strains 1, 2 and 3 isolated from cassava dumpsites were used for the production of amylase enzyme. The Aspergillus niger strains 1, 2 and 3 had diameter (mm) zone of clearance of 17.0, 23.0 and 8.0 respectively using Potato dextrose agar plates fortified with starch. Studies on the amylase enzyme activity (mg/ml) of Aspergillus niger strains 1 and 2 showed 19,340 and 16,510 respectively. These values were higher than the commercially available amylase enzyme that had an activity of 5,722.2. The protein (mg/ml) and specific activity (units/mg) for amylase from Aspergillus niger strain 1 was 28.39 and 681.23 while 21.76 and 758.73 from Aspergillus niger 2 respectively. Purification using ammonium sulphate (% w/v) at 60, 80 and 100 on amylase enzyme from Aspergillus niger strain 1 for enzyme activity, protein and specific activity was 44405.49, 17.01 and 2610.55, 28949.76, 23.62 and 1225.65, 36220.25, 16.67, and 2172.787 respectively. The microbial production of Amylase enzyme in Nigeria from Cassava peel will reduce cost of production, convert cassava peel from waste condition to wealth, and will boost economy through indigenous industrialization

    Production and Partial Purification of Amylase By Aspergillus niger Isolated from Cassava Peel

    No full text
    Aspergillus niger strains 1, 2 and 3 isolated from cassava dumpsites were used for the production of amylase enzyme. The Aspergillus niger strains 1, 2 and 3 had diameter (mm) zone of clearance of 17.0, 23.0 and 8.0 respectively using Potato dextrose agar plates fortified with starch. Studies on the amylase enzyme activity (mg/ml) of Aspergillus niger strains 1 and 2 showed 19,340 and 16,510 respectively. These values were higher than the commercially available amylase enzyme that had an activity of 5,722.2. The protein (mg/ml) and specific activity (units/mg) for amylase from Aspergillus niger strain 1 was 28.39 and 681.23 while 21.76 and 758.73 from Aspergillus niger 2 respectively. Purification using ammonium sulphate (% w/v) at 60, 80 and 100 on amylase enzyme from Aspergillus niger strain 1 for enzyme activity, protein and specific activity was 44405.49, 17.01 and 2610.55, 28949.76, 23.62 and 1225.65, 36220.25, 16.67, and 2172.787 respectively. The microbial production of Amylase enzyme in Nigeria from Cassava peel will reduce cost of production, convert cassava peel from waste condition to wealth, and will boost economy through indigenous industrialization
    corecore