Glucoamylase is an enzyme that hydrolyses 1,4α and 1,6β-glucosidic linkages in polysaccharides yielding glucose. Aspergillus niger strains 1, 2 and 3 were locally isolated from cassava peel dumpsite for the production of glucoamylase enzyme. A. niger strains 1, 2 and 3 were screened for their hyper producing ability on potato dextrose agar using plate assay method fortified with starch agar, and showed zone of clearance of 17.0, 23.0 and 8.0 mm, respectively. The glucoamylase activity for A. niger strains 1 and 2 were 13 000.0 and 11 740.0, respectively. These values were however higher than the activity as obtained from the commercial enzyme with 2 500.0. Investigations on the protein (mg/ml), and specific activity (units/mg) on glucoamylase produced by A. niger strains 1 and 2 was 24.20, 537.19, 23.13 and 507.57, respectively. Fractionation of the enzyme ammonium sulphate (% w/v) using 60, 80 and 100% showed that the enzyme activities were 33 179.86, 47 985.86 and 19 167.65 units/ml, respectively. Protein concentrations were 16.29, 16.29 and 21.55 units/mg, respectively, while specific activities were 2 036.82, 2 945.725 and 889.45 units/mg, respectively. The production, packaging, and commercialization of glucoamylase in Nigeria will save a lot of foreign exchange earnings, and boost the economy of Nigeria.
Pectinases accelerate the breakdown of the glycosidic bonds in pectin into simpler forms. Pectinases in the study were produced using three extraction solvents, three fungi, and six substrates. Citrate buffer, distilled water and 0.1 M NaCl were utilized as extraction solvents. Penicillium sp, Pichia kudriavzevii F2-T429-5 and Aspergillus niger were selectively isolated from the environment and identified. The substrates include; wheat bran, banana peels, orange peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves in solid-state fermentation. The dinitro salicylic acid (DNS) technique was used to determine pectinase activity. In comparison to distilled water, the study found that extracting the enzyme from the fermentation medium with 0.1 M NaCl solvent resulted in considerable (p<0.05) activity. The best substrate and fungus were orange peels and Aspergillus niger, respectively. In general, when compared to the yeast Pichia kudriavzevii F2-T429-5, the molds (Penicillium sp. and Aspergillus niger) produced pectinases with higher activity. Orange peel resulted in pectinase production with significant (p<0.05) activity compared to wheat bran, banana peels, corn cobs, Thaumatococcus daniellii (sweet prayer plant) fruit peels, and leaves. Additionally, Pichia kudriavzevii F2-T429-5 in Thaumatococcus daniellii fruit peel fermentation produced pectinase with the lowest activity. The inference drawn from the study shows the potential of T. daniellii fruit peels, its leaves, and Pichia kudriavzevii F2-T429-5 for pectinase production.
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