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1.
Opt Express ; 31(14): 22444-22456, 2023 Jul 03.
Article in English | MEDLINE | ID: mdl-37475355

ABSTRACT

Geometrical gain of a luminescent solar concentrator is drastically increased by laying out a luminescent fiber in a luminescent plate with air gap around it and attaching a photovoltaic (PV) cell to the tip of the fiber. The plate converts an incident photon to a first photoluminescence (PL) photon, and the fiber converts it to a second PL photon. Thus, the fiber carries the optical power as a leaf vein transports water and nutrients. The probability of the first PL photon resulting in the second PL photon reaching the PV cell can be measured by exciting a single spot on the plate with a laser beam. In experiment, 2 mm-thick, 50 mm-square and 50 mm-diameter circular devices were assembled with off-the-shelf components. For each case, geometrical gain exceeded 1000 and this probability averaged over the incident area was of the order of 0.01. Connecting multiple small-area devices to a single PV cell with a clear fiber would increase geometrical gain further and alleviate the absorption and scattering of PL photons during waveguiding.

2.
Opt Express ; 29(22): 36784-36795, 2021 Oct 25.
Article in English | MEDLINE | ID: mdl-34809081

ABSTRACT

One can display images and harvest energy by utilizing ambient light with a stack of an optical shutter array, a luminescent layer and a solar cell. In our experiment, a luminescent layer and a corresponding color filter were attached to a polycrystalline Si solar cell with 13% power conversion efficiency. For each configuration using BBOT, Coumarin 6 and Lumogen F Red 305, the power conversion efficiency was measured to be 6.7%, 8.0% and 8.9%, respectively. The luminance of these configurations was proportional to the illuminance in all cases. Its color gamut was comparable to the National Television System Committee standard.

3.
J Biosci Bioeng ; 127(5): 582-588, 2019 May.
Article in English | MEDLINE | ID: mdl-30401585

ABSTRACT

Thermophilic methane fermentation was a valid approach for handling the stillage eluted from ethanol fermentation of waste paper and kitchen waste. The wide organic loading rate (OLR) range (2-14 g VTS/(L d)) for stable performance and relatively high energy recovery efficiency (79.0%) were achieved, and OLR of 8 g VTS/(L d) was optimum for achievement of highest biogas evolution and VTS removal efficiency. Microbial community analysis revealed that hydrolysis of cellulose was the critical step for methane production from the stillage.


Subject(s)
Bacteria/metabolism , Ethanol/metabolism , Methane/biosynthesis , Waste Products/analysis , Anaerobiosis , Biodegradation, Environmental , Biofuels/analysis , Bioreactors , Cellulose/chemistry , Cellulose/metabolism , Ethanol/chemistry , Fermentation , Hydrolysis , Paper
4.
Waste Manag ; 76: 404-413, 2018 Jun.
Article in English | MEDLINE | ID: mdl-29625877

ABSTRACT

To investigate the effect of delignification on enzymatic saccharification and ethanol fermentation of sugarcane bagasse (SCB), NaClO, NaOH, and Na2CO3 were used to prepare SCB with different lignin contents. We found that a lignin content of approximately 11% was sufficient for enzymatic saccharification and fermentation. Based on this result, an economical delignification pretreatment method using a combination of acid and alkali (CAA) was applied. Lignin content of 11.7% was obtained after CAA pretreatment with 0.5% w/v H2SO4 at 140 °C for 10 min and 1.0% w/v NaOH at 90 °C for 60 min. Presaccharification-simultaneous saccharification and fermentation (P-SSF) of the CAA-pretreated SCB resulted in an ethanol concentration of 43.8 g/L and an ethanol yield of 81.7%, with an enzyme loading of 15 FPU/g-CAA-pretreated SCB. Enzyme activities (filter paper, carboxymethyl cellulase, and ß-glucosidase activities) were determined in liquid phase during P-SSF, indicating that the residual cellulase activity could be further used. Thus, fed-batch P-SSF was carried out, and an ethanol concentration of 43.1 g/L and an ethanol yield of 80.4% were obtained with an enzyme loading of 10 FPU/g-CAA-pretreated SCB. Fed-batch P-SSF was found to be effective to reduce enzyme loading.


Subject(s)
Bioreactors , Cellulose/metabolism , Lignin/analysis , Cellulase , Ethanol , Fermentation , Hydrolysis , Saccharum
5.
Waste Manag ; 67: 86-94, 2017 Sep.
Article in English | MEDLINE | ID: mdl-28527862

ABSTRACT

Efficient ethanol production from waste paper requires the addition of expensive nutrients. To reduce the production cost of ethanol from waste paper, a study on how to produce ethanol efficiently by adding kitchen waste (potentially as a carbon source, nutrient source, and acidity regulator) to waste paper was performed and a process of successive liquefaction, presaccharification, and simultaneous saccharification and fermentation (L+PSSF) was developed. The individual saccharification performances of waste paper and kitchen waste were not influenced by their mixture. Liquefaction of kitchen waste at 90°C prior to presaccharification and simultaneous saccharification and fermentation (PSSF) was essential for efficient ethanol fermentation. Ethanol at concentrations of 46.6 or 43.6g/l was obtained at the laboratory scale after fermentation for 96h, even without pH adjustment and/or the addition of extra nutrients. Similarly, ethanol at a concentration of 45.5g/l was obtained at the pilot scale after fermentation for 48h. The ethanol concentration of L+PSSF of the mixture of waste paper and kitchen waste was comparable to that of PSSF of waste paper with added nutrients (yeast extract and peptone) and pH adjustment using H2SO4, indicating that kitchen waste is not only a carbon source but also an excellent nutrient source and acidity regulator for fermentation of the mixture of waste paper and kitchen waste.


Subject(s)
Ethanol , Paper , Saccharomyces cerevisiae , Biofuels , Fermentation , Refuse Disposal
6.
Waste Manag ; 48: 644-651, 2016 Feb.
Article in English | MEDLINE | ID: mdl-26687227

ABSTRACT

Waste paper can serve as a feedstock for ethanol production due to being rich in cellulose and not requiring energy-intensive thermophysical pretreatment. In this study, an efficient process was developed to convert waste paper to ethanol. To accelerate enzymatic saccharification, pH of waste paper slurry was adjusted to 4.5-5.0 with H2SO4. Presaccharification and simultaneous saccharification and fermentation (PSSF) with enzyme loading of 40 FPU/g waste paper achieved an ethanol yield of 91.8% and productivity of 0.53g/(Lh) with an ethanol concentration of 32g/L. Fed-batch PSSF was used to decrease enzyme loading to 13 FPU/g waste paper by feeding two separate batches of waste paper slurry. Feeding with 20% w/w waste paper slurry increased ethanol concentration to 41.8g/L while ethanol yield decreased to 83.8%. To improve the ethanol yield, presaccharification was done prior to feeding and resulted in a higher ethanol concentration of 45.3g/L, a yield of 90.8%, and productivity of 0.54g/(Lh). Ethanol fermentation recovered 33.2% of the energy in waste paper as ethanol. The biochemical methane potential of the stillage eluted from ethanol fermentation was 270.5mL/g VTS and 73.0% of the energy in the stillage was recovered as methane. Integrating ethanol fermentation with methane fermentation, recovered a total of 80.4% of the energy in waste paper as ethanol and methane.


Subject(s)
Ethanol/chemistry , Fermentation , Methane/chemistry , Paper , Recycling/methods , Refuse Disposal/methods , Anti-Bacterial Agents/chemistry , Biofuels , Cellulase/chemistry , Cellulose/metabolism , Conservation of Natural Resources , Hydrogen-Ion Concentration , Hydrolysis , Industrial Microbiology , Saccharomyces cerevisiae , Temperature , beta-Glucosidase/metabolism
7.
J Biol Chem ; 289(23): 15957-67, 2014 Jun 06.
Article in English | MEDLINE | ID: mdl-24755225

ABSTRACT

The lack of a few conserved enzymes in the classical mevalonate pathway and the widespread existence of isopentenyl phosphate kinase suggest the presence of a partly modified mevalonate pathway in most archaea and in some bacteria. In the pathway, (R)-mevalonate 5-phosphate is thought to be metabolized to isopentenyl diphosphate via isopentenyl phosphate. The long anticipated enzyme that catalyzes the reaction from (R)-mevalonate 5-phosphate to isopentenyl phosphate was recently identified in a Cloroflexi bacterium, Roseiflexus castenholzii, and in a halophilic archaeon, Haloferax volcanii. However, our trial to convert the intermediates of the classical and modified mevalonate pathways into isopentenyl diphosphate using cell-free extract from a thermophilic archaeon Thermoplasma acidophilum implied that the branch point intermediate of these known pathways, i.e. (R)-mevalonate 5-phosphate, is unlikely to be the precursor of isoprenoid. Through the process of characterizing the recombinant homologs of mevalonate pathway-related enzymes from the archaeon, a distant homolog of diphosphomevalonate decarboxylase was found to catalyze the phosphorylation of (R)-mevalonate to yield (R)-mevalonate 3-phosphate. The product could be converted into isopentenyl phosphate, probably through (R)-mevalonate 3,5-bisphosphate, by the action of unidentified T. acidophilum enzymes fractionated by anion-exchange chromatography. These findings demonstrate the presence of a third alternative "Thermoplasma-type" mevalonate pathway, which involves (R)-mevalonate 3-phosphotransferase and probably both (R)-mevalonate 3-phosphate 5-phosphotransferase and (R)-mevalonate 3,5-bisphosphate decarboxylase, in addition to isopentenyl phosphate kinase.


Subject(s)
Mevalonic Acid/analogs & derivatives , Mevalonic Acid/metabolism , Thermoplasma/metabolism , Adenosine Triphosphate/metabolism , Archaeal Proteins/genetics , Archaeal Proteins/metabolism , Base Sequence , Cell-Free System , Chromatography, Ion Exchange , Chromatography, Thin Layer , DNA Primers , Phylogeny
8.
Prep Biochem Biotechnol ; 43(7): 682-95, 2013.
Article in English | MEDLINE | ID: mdl-23768113

ABSTRACT

Corn stover is the most abundant agricultural residue in China and a valuable reservoir for bioethanol production. In this study, we proposed a process for producing bioethanol from corn stover; the pretreatment prior to presaccharification, followed by simultaneous saccharification and fermentation (SSF) by using a flocculating Saccharomyces cerevisiae strain, was optimized. Pretreatment with acid-alkali combination (1% H2SO4, 150 °C, 10 min, followed by 1% NaOH, 80°C, 60 min) resulted in efficient lignin removal and excellent recovery of xylose and glucose. A glucose recovery efficiency of 92.3% was obtained by enzymatic saccharification, when the pretreated solid load was 15%. SSF was carried out at 35 °C for 36 hr after presaccharification at 50 °C for 24 hr, and an ethanol yield of 88.2% was achieved at a solid load of 15% and an enzyme dosage of 15 FPU/g pretreated corn stover.


Subject(s)
Ethanol/chemical synthesis , Fermentation , Sodium Hydroxide/chemistry , Sulfuric Acids/chemistry , Zea mays/chemistry , Biotechnology/methods , Glucose/chemistry , Glucose/metabolism , Hydrolysis , Lignin/chemistry , Saccharomyces cerevisiae/chemistry , Saccharomyces cerevisiae/metabolism
9.
J Biochem ; 153(5): 415-20, 2013 May.
Article in English | MEDLINE | ID: mdl-23378249

ABSTRACT

The existence of the classical mevalonate (MVA) pathway was examined in the thermoacidophilic archaeon Sulfolobus solfataricus. The pathway is considered uncommon among archaea because the genes of the orthologues of phosphomevalonate kinase (PMK) and/or diphosphomevalonate decarboxylase (DMD) are absent in the genomes of most archaea. Instead, the modified MVA pathway, which involves isopentenyl phosphate kinase (IPK), has been proposed to exist in the archaea that lack the classical pathway. However, some archaea including S. solfataricus possess the genes of the orthologues of both IPK and all enzymes of the classical pathway. Biochemical characterization using recombinant proteins showed that the orthologues of the enzymes catalyzing the late steps of the classical pathway, i.e. MVA kinase, PMK and DMD, are all active. Moreover, in vitro conversion of the intermediates in the classical and modified pathways by cell-free extract from S. solfataricus indicated that only the classical pathway likely works in the organism.


Subject(s)
Mevalonic Acid/metabolism , Sulfolobus solfataricus/metabolism , Models, Biological , Phosphotransferases (Phosphate Group Acceptor)/metabolism , Protein Kinases/metabolism , Signal Transduction/physiology , Terpenes/metabolism
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