11 research outputs found
MOESM1 of Predicting the most appropriate wood biomass for selected industrial applications: comparison of wood, pulping, and enzymatic treatments using fluorescent-tagged carbohydrate-binding modules
Additional file 1: Table S1. Protein content and activities of the two commercial enzyme mixtures. Enzyme cocktail T refers to CelluClast 1.5L from Trichoderma reesei and enzyme cocktail A refers to Carezyme 1000L from Aspergillus sp
Isolation of High-Purity Cellulose Nanofibers from Wheat Straw through the Combined Environmentally Friendly Methods of Steam Explosion, Microwave-Assisted Hydrolysis, and Microfluidization
High-purity cellulose
nanofibers were isolated from wheat straw
through an environmentally friendly, multistep treatment process that
combined steam explosion, microwave-assisted hydrolysis, and microfluidization.
The cellulose content of the processed nanofibers increased from 44.81%
to 94.23%, whereas the hemicellulose and lignin contents significantly
decreased. Scanning electron microscopy revealed the effects of the
isolation treatments on fiber morphology and width. Atomic force microscopy
was used to observe the changes in the components, surface roughness,
and crystallinity of the fibers. Transmission electron microscopy
showed long, loose nanofiber bundles that were 10â40 nm wide
with an average individual diameter of 5.42 nm. Fourier transform
infrared spectroscopy showed that noncellulosic components were effectively
removed. X-ray diffraction analysis revealed the improved crystallinity
of the processed fibers, as well as the partial crystalline transformation
of cellulose I to cellulose II. Thermogravimetric analysis and derivative
thermogravimetric results showed the enhanced thermal properties of
the nanofibers. The removal of hemicellulose and lignin increased
the crystallinity of the fibers, thus enhancing the thermal properties
of the processed fibers. Results indicated that the efficient, environmentally
friendly, multistep treatment process yields nanofibers with potential
advanced applications
Quantification of methanol-soluble luteolin, chrysoeriol, selgin, and tricin extracted from the biomass of wild-type (WT) and <i>bmr12</i> sorghum lines.
<p>Values in <i>bmr12</i> are expressed as a percentage of the values measured in wild-type extracts which correspond to 317 ± 4 ”g/g dry weight (DW) for luteolin, 7.8 ± 0.0 ”g/g DW for chrysoeriol, 2.0 ± 0.2 ”g/g DW for selgin, and 274 ± 3 ”g/g DW for tricin. Error bars represent the standard deviation from five experimental replicates. Asterisks indicate significant differences from the wild-type using the unpaired Studentâs t-test (*<i>P</i> < 0.05).</p
Amount of tricin in cellulolytic lignin purified from wild-type (WT) and <i>bmr12</i> sorghum lines.
<p>Tricin was released from lignin using the thioacidolysis procedure and subsequently quantified by HPLC-ESI-TOF MS. Error bars represent the standard deviation from three experimental replicates. Asterisks indicate a significant difference from the wild-type using the unpaired Studentâs t-test (*<i>P</i> < 0.05).</p
Lignin monomeric composition in wild-type (WT) and <i>bmr12</i> sorghum biomass.
<p>For each genotype, cellulolytic lignin was isolated and analyzed by 2D <sup>13</sup>Câ<sup>1</sup>H HSQC NMR spectroscopy. Regions of partial short-range <sup>13</sup>Câ<sup>1</sup>H HSQC spectra are shown. Lignin monomer ratios including tricin (T) are provided on the figures. S: syringyl, G: guaiacyl, 5OH-G: 5-hydroxyguaiacyl, H: <i>p</i>-hydroxyphenyl, <i>p</i>CA: <i>p</i>-coumarate, FA: ferulate.</p
Simplified representation of the lignin and tricin biosynthetic pathways from phenylalanine.
<p>Abbreviations are: Bmr12, Brown midrib12; OMT, <i>O</i>-methyltransferase; SbCOMT, <i>Sorghum bicolor</i> caffeate <i>O</i>-methyltransferase.</p
Expression of genes involved in subcutaneous adipose tissue metabolism.
<p>GPR43, G protein-coupled receptor 43 (A). aP2, adipocyte fatty acid binding protein (B). FAS, fatty acid synthase (C). HSL, hormone-sensitive lipase (D). MGL, monoglycerol lipase (E). ZAG, zinc-a2 glycoprotein (F). CPT1a, carnitine palmitoyltransferase 1a (G). PGC1α, PPARγ coactivator 1 alpha (H). ACO, acyl-CoA oxidase (I). Data with different superscript letters are significantly different.</p
Changes in microbial diversity and populations in the caecal content, assessed by 454-pyrosequencing.
<p>Microbial diversity indexes (A). Principal component analysis based on the relative abundance distribution at the species level (B). Relative abundances of bacterial taxa accounting for more than 1%, at the phylum, family and genus levels (C). Relative abundances of the Bacteroidetes phylum, <i>Bacteroidaceae</i> family, <i>Bacteroides</i> genus and species-like <i>Bacteroides</i> HQ788586 (D). Data with different superscript letters are significantly different.</p
Body and tissue weight, portal serum parameters and hepatic lipids.
<p>Data are mean ± SEM. Data with different superscript letters are significantly different.</p><p>Body and tissue weight, portal serum parameters and hepatic lipids.</p
Short chain fatty acid (SCFA) profile in the caecal content.
<p>Acetate (A). Propionate (B). Butyrate (C). Valerate (D). Isovalerate (E). Isobutyrate (F). Caproate (G). Branched SCFA (H). Total SCFAs (I). Data with different superscript letters are significantly different.</p