Amylase is essential in the industrial sector, but there are some challenges with its low reusability efficiency. The catalytic activity of the amylase can be affected by using an activated carbon matrix as an immobilization technique. In this study, we characterized the purified amylase of Aspergillus niger ICP2 and immobilized it to activated carbon. Amylase production from A. niger ICP2 was performed throughout a 7-day incubation. After partial purification, two amylase fractions were generated, including 90% saturation ammonium sulfate precipitation, a 10-kDa hollow fiber dialysis column, and anion exchange chromatography. Thin-layer chromatography analysis showed the presence of glucose in fractions I and II, indicating glucoamylase activity. Both fractions had optimum pH and temperatures at 4.5 and 70°C, respectively. Fraction I was stable at acidic pH (3.5-5), while the stability of fraction II was in the range of acid to base (4-7.5) after incubation for 1 hour at 37°C. Both fractions displayed the same pattern of temperature stability (30-50°C) when incubated for 1 hour at optimum buffer. Activated carbon was used to immobilize amylase fraction II, which demonstrated the ability to hydrolysis the starch up to five times with a reduction in the activity of 50.4%. These results showed promising hydrolysis reusability by amylase immobilized using activated carbon.
An α-1,4-glycosidic bonds galactoses pectin, mainly composed of a D-galacturonic acid chain, are important biomaterial widely used in industries. Utilizing this material, a bioprocess, including the biocatalysis pectinase, is often needed. Pectinase production was optimized in 7 days SSF at 37°C, and the pectinase activities were daily measured by the method of Somogy-Nelson. The optimum pectinase production was 0.166 U/ml on the fourth day SSF. Purification using open column ion exchange chromatography DEAE cellulose DE-52 resulted in 1030.9 folds of pectinase purity with a yield of 25.9%. The enzyme was at optimal activity at pH six and attended stable in the pH range of 5.5-8, while optimal activity at a temperature of 50°C and was stable in the range of 30-45°C. The pectinase activity increased by 120% with the addition of 10 mM Mg2+, and 95% retained when 10 mM Ca2+ was added. The presence of 10 mM Na+, K+, and Fe2+ resulted in a slight effect of activity at 85%, 83%, and 78%. However, it was strongly inhibited by 10 mM Al3+ and retained 25%. Based on the results above, the microbial utilization of coffee pulp waste by ISH16 bacteria pectinolytic is one opportunity to produce valuable pectinase with low-cost production, so comprehensive examination in large-scale production is needed too. In this paper, all research detail steps were described.
The future applications of amylase have sparked the interest of several industries, resulting in the discovery of possible amylase-producing microbes. Aspergillus niger ICP2 was an indigenous fungus isolated from coffee pulp that shows amylolytic activity after growing on a soluble starch agar. In this study, we optimized the production and successfully purified the amylase from Aspergillus niger ICP2. Amylase optimization production was performed for a 7-day of incubation under submerged fermentation. The amylase activity was measured using the iodin method, and the total protein was quantified spectrophotometrically at 280 nm. Purifying amylase crude extract conducted such as ammonium sulfate precipitation, dialysis, and anion-exchange chromatography. Amylase was maximally precipitated at 90% saturation, followed by dialysis on a 10 kDa column, increasing specific activity up to 12.17 U/mg and purity multiples of 9.31 times. Two peaks of amylase activity were formed when the dialyzed amylase was loaded onto anion exchange chromatography with specific activities of 14.47 U/mg (fraction I) and 32.73 U/mg (fraction II). The increase in specific activity and purity fold indicated that the amylase purification process was successful.
These articles have been peer-reviewed by the members of the Scientific Committee of ICOLIB and approved by the Editor-in-Chief, who affirms that this document is a truthful description of the conference's review process. Review ProcedureThe reviews were double-blind. Each submission was examined by two reviewer(s) independently. The conference submission management system was easy chair.We divided the submission of the ICOLIB participant into two categories, the first is abstract and the second the full manuscript submission. The submissions of the abstract were first screened for generic quality, relatedness to the main topic and suitableness by the editorial team. Based on this initial screening, all of the abstracts would be classified by the main theme, i.e. Applied Sciences (Agriculture, Biotechnology & Bioinformatics), Basic Sciences (Ecology, Zoology, Botany, and Microbiology), Biodiversity & Bioconservation, Health & Medicine (Pharmacy & Medical Sciences). All of the selected abstracts would be presented by their author during the ICOLIB conferences. The committee gave an option to the authors to publish their manuscripts or just presented their work in the ICOLIB conference.All of the complete manuscripts then follow the review process, the first step was to evaluate the relatedness to the proceedings series "Advances in Biological Sciences Research", scientific quality, novelty and contribution to the science. The second step is checking the similarity using Turnitin to evaluate the textual overlap and detect the possible sign of plagiarism. The third step was to send for peer review by matching each B.
Microbial utilization of agricultural biomass wastes has been widely used to synthesize certain an enzyme. We previously investigated that cellulase can be produced under solid stated fermentation based on coffee pulp waste substrate using Aspergillus sp. VTM1. Crude cellulase production was optimized for a week of incubation at 30 °C, the crude was harvested daily with distilled water containing 1% NaCl and 0.1% NaN3. To measure cellulase activity, the reducing sugar Somogy-Nelson method was used. In the next step, crude cellulase was dialyzed using a 45μm cellulose membrane tube 12-14 kDa against acetate buffer pH 5. Further analysis found that the maximum activity of cellulase production was obtained after inoculating 10 8 spores/ml of Aspergillus sp. VTM1 to the 5g of sterile coffee pulp (67% humidity) at 30 °C for 96 h. Large-scale production of cellulase crude extract results in an activity of 0.70 U/ml with a total activity of 121.1 U/ml. After the dialysis, the enzyme activity (0.81 U/ml) and specific activity (0.01 U/mg) were increased compared to the crude extract. On an anion exchanger using DEAE cellulose DE-52, the specific activity was 0.1 U/mg, increased 25.03 times with a yield of 36,82%. The findings of this study lead to a green strategy for cellulase production under solid-state fermentation by Aspergillus sp. VTM1 and its purification.
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