KINETIC STUDY ON HYDROTHERMAL COMPOSITION OF GLUCOSE IN NAOH SOLUTION WITH ZNO AS CATALYST

<p>Hydrothermal liquifaction is a biomass conversion process, where the structure of the biomass is convert into liquid components under super critical conditions with a high temperature. In this study, glucose is used as biomass. The purpose of this study was to study the reaction kinetics and determine the hydrothermal decomposition of glucose in NaOH solution. This experiment used 10 grams of glucose and dissolve it in 80 mL of NaOH solution then put it in an autoclave. Experiments were carried out by varying the heating temperature carried out in an autoclave with a magnetic stirrer. After heating at various temperatures, the autoclave is immediately cooled down. The processed material is filtered to separate insoluble solids from the liquid phase. The solid residue that has been separated from the liquid phase is then dried in an oven at 105°C for 24 hours. The composition of the filtrate was analyzed using the GC-MS method and the glucose concentration was analyzed using the Lane Eynon method. Prior to GC-MS analysis, the filtrate was distilled at atmospheric pressure until a solid residue remained. The sample analyzed is the result of distillation with a temperature above 100°C to ensure that there is no water and residual glucose in the sample. The results of GC-MS analysis of product samples from the hydrothermal decomposition process had 3 peaks. The first peak shows the compound 1,3 Dipalmitin which has an area of 14.74%, the second peak shows the Olealdehyde compound which has an area of 32.35%, and the third peak shows the 1,2-Epoxyhexadecane compound which has an area of 52.91%. The kinetics results in hydrothermal decomposition of glucose in this experiment obtained a reaction order of 2 with an activation energy (Ea) of 15.91 KJ / mol and a pre-exponential factor of 66.12.</p>

Recombinant bacteriophage LysKB317 endolysin mitigates Lactobacillus infection of corn mash fermentations

Background Commercial ethanol fermentation facilities traditionally rely on antibiotics for bacterial contamination control. Here we demonstrate an alternative approach to treat contamination using a novel peptidoglycan hydrolase (LysKB317) isolated from a bacteriophage, EcoSau. This endolysin was specially selected against Lactobacillus strains that were isolated as contaminants from a fuel ethanol plant. The LysKB317 gene was recombinantly expressed in Escherichia coli as a 33 kDa purified enzyme. Results In turbidity reduction assays, the recombinant enzyme was subjected to a panel of 32 bacterial strains and was active against 28 bacterial strains representing 1 species of Acetobacter, 8 species of Lactobacillus, 1 species of Pediococcus, 3 species of Streptococcus, and 1 species of Weissella. The activity of LysKB317 was optimal around pH 6, but it has broad activity and stability from pH 4.5–7.5 up to at least 48 h. Maximum activity was observed at 50 °C up to at least 72 h. In addition, LysKB317 was stable in 30% ethanol up to at least 72 h. In experimentally infected corn mash fermentations, 1 µM endolysin reduced bacterial load by 3-log fold change, while 0.01 µM reduced bacteria by 2-log fold change. Concentration of fermentation products (ethanol, residual glucose, lactic acid, and acetic acids) for infected cultures treated with ≥ 0.01 µM LysKB317 was similar to uncontaminated controls. Conclusion Exogenously added LysKB317 endolysin is functional in conditions typically found in fuel ethanol fermentations tanks and may be developed as an alternative to antibiotics for contamination control during fuel ethanol fermentations.

Recombinant Bacteriophage LysKB317 Endolysin Mitigates Lactobacillus Infection of Corn Mash Fermentations

Background Commercial ethanol fermentation facilities traditionally rely on antibiotics for bacterial contamination control. Here we demonstrate an alternative approach to treat contamination using a novel peptidoglycan hydrolase (LysKB317) isolated from a bacteriophage, EcoSau. This endolysin was specially selected against Lactobacillus strains that were isolated as contaminants from a fuel ethanol plant. The LysKB317 gene was recombinantly expressed in Escherichia coli as a 33 kDa purified enzyme. Results In turbidity reduction assays, the recombinant enzyme was subjected to a panel of 32 bacterial strains and was active against 28 bacterial strains representing one species of Acetobacter, eight species of Lactobacillus, one species of Pediococcus, three species of Streptococcus, and one species of Weissella. The activity of LysKB317 was optimal around pH 6, but it has broad activity and stability from pH 4.5 – 7.5 up to at least 48 h. Maximum activity was observed at 50°C up to at least 72 hrs. In addition, LysKB317 was stable in 30% ethanol up to at least 72 hrs. In experimentally infected corn mash fermentations, 1 µM endolysin reduced bacterial load by 3-log fold change, while 0.01 µM reduced bacteria by 2-log fold change. Concentration of fermentation products (ethanol, residual glucose, lactic acid, and acetic acids) for infected cultures treated with ≥ 0.01 µM LysKB317 were similar to uncontaminated controls. Conclusion Exogenously added LysKB317 endolysin is functional in conditions typically found in fuel ethanol fermentations tanks and may be developed as an alternative to antibiotics for contamination control during fuel ethanol fermentations.

Recombinant Bacteriophage LysKB317 Endolysin Mitigates Lactobacillus Infection of Corn Mash Fermentations

Background Commercial ethanol fermentation facilities traditionally rely on antibiotics for bacterial contamination control. Here we demonstrate an alternative approach to treat contamination using a novel peptidoglycan hydrolase (LysKB317) isolated from a bacteriophage, EcoSau. This endolysin was specially selected against Lactobacillus strains that were isolated as contaminants from a fuel ethanol plant. The LysKB317 gene was recombinantly expressed in Escherichia coli as a 33 kDa purified enzyme. Results In turbidity reduction assays, the recombinant enzyme was subjected to a panel of 32 bacterial strains and was active against 28 bacterial strains representing one species of Acetobacter, eight species of Lactobacillus, one species of Pediococcus, three species of Streptococcus, and one species of Weissella. The activity of LysKB317 was optimal around pH 6, but it has broad activity and stability from pH 4.5 – 7.5 up to at least 48 h. Maximum activity was observed at 50°C up to at least 72 h. In addition, LysKB317 was stable in 30% ethanol up to at least 72 h. In experimentally infected corn mash fermentations, 1 µM endolysin reduced bacterial load by 4-log fold change, while 0.01 µM reduced bacteria by 2-log fold change. Concentration of fermentation products (ethanol, residual glucose, lactic acid, and acetic acids) for infected cultures treated with ≥ 0.01 µM LysKB317 were similar to uncontaminated controls. Conclusion Exogenously added LysKB317 endolysin is functional in conditions typically found in fuel ethanol fermentations tanks and may be developed as an alternative to antibiotics for contamination control during fuel ethanol fermentations.