| 1. |
- Mohan Pawar, Prashant, et al.
(författare)
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In muro deacetylation of xylan affects lignin properties and improves saccharification of aspen wood
- 2017
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Ingår i: Biotechnology for Biofuels. - : Springer Science and Business Media LLC. - 1754-6834 .- 1754-6834. ; 10:1, s. Art nr 98-
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Tidskriftsartikel (refereegranskat)abstract
- Background: Lignocellulose from fast growing hardwood species is a preferred source of polysaccharides for advanced biofuels and "green" chemicals. However, the extensive acetylation of hardwood xylan hinders lignocellulose saccharification by obstructing enzymatic xylan hydrolysis and causing inhibitory acetic acid concentrations during microbial sugar fermentation. To optimize lignocellulose for cost-effective saccharification and biofuel production, an acetyl xylan esterase AnAXE1 from Aspergillus niger was introduced into aspen and targeted to cell walls. Results: AnAXE1-expressing plants exhibited reduced xylan acetylation and grew normally. Without pretreatment, their lignocellulose yielded over 25% more glucose per unit mass of wood (dry weight) than wild-type plants. Glucose yields were less improved (+7%) after acid pretreatment, which hydrolyses xylan. The results indicate that AnAXE1 expression also reduced the molecular weight of xylan, and xylan-lignin complexes and/or lignin co-extracted with xylan, increased cellulose crystallinity, altered the lignin composition, reducing its syringyl to guaiacyl ratio, and increased lignin solubility in dioxane and hot water. Lignin-associated carbohydrates became enriched in xylose residues, indicating a higher content of xylo-oligosaccharides. Conclusions: This work revealed several changes in plant cell walls caused by deacetylation of xylan. We propose that deacetylated xylan is partially hydrolyzed in the cell walls, liberating xylo-oligosaccharides and their associated lignin oligomers from the cell wall network. Deacetylating xylan thus not only increases its susceptibility to hydrolytic enzymes during saccharification but also changes the cell wall architecture, increasing the extractability of lignin and xylan and facilitating saccharification.
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| 3. |
- Parikka, K., et al.
(författare)
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Functional and anionic cellulose-interacting polymers by selective chemo-enzymatic carboxylation of galactose-containing polysaccharides
- 2012
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Ingår i: Biomacromolecules. - : American Chemical Society (ACS). - 1525-7797 .- 1526-4602. ; 13:8, s. 2418-2428
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Tidskriftsartikel (refereegranskat)abstract
- Carboxylated, anionic polysaccharides were selectively prepared using a combination of enzymatic and chemical reactions. The galactose-containing polysaccharides studied were spruce galactoglucomannan, guar galactomannan, and tamarind galactoxyloglucan. The galactosyl units of the polysaccharides were first oxidized with galactose oxidase (EC 1.1.3.9) and then selectively carboxylated, resulting in the galacturonic acid derivatives with good conversion and yield. The degrees of oxidation (DO) of the products were determined by gas chromatography-mass spectrometry (GC-MS). A novel feasible electrospray ionization-mass spectrometry (ESI-MS) method was also developed for the determination of DO. The solution properties and charge densities of the products were investigated. The interaction of the products with cellulose was studied by two methods, bulk sorption onto bleached birch kraft pulp and adsorption onto nanocellulose ultrathin films by quartz crystal microbalance with dissipation (QCM-D). To study the effect of the location of the carboxylic acid groups on the physicochemical properties, polysaccharides were also oxidized by 2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO)-mediated reaction producing polyuronic acids. The chemo-enzymatically oxidized galacturonic polysaccharides with an unmodified backbone had a better ability to interact with cellulose than the TEMPO-oxidized products. The selectively carboxylated polysaccharides can be further exploited, as such, or in the targeted functionalization of cellulose surfaces.
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| 4. |
- Ademark, Pia, et al.
(författare)
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Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J. Biotechnol. 75: 281-289.
- 1999
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Ingår i: Journal of Biotechnology. - 1873-4863. ; 75:2-3, s. 281-289
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Tidskriftsartikel (refereegranskat)abstract
- A β-mannosidase was purified to homogeneity from the culture filtrate of Aspergillus niger. A specific activity of 500 nkat mg−1 and a 53-fold purification was achieved using ammonium sulfate precipitation, anion-exchange chromatography, and gel filtration. The isolated enzyme has an isoelectric point of 5.0 and appears to be a dimer composed of two 135-kDa subunits. It is a glycoprotein and contains 17% N-linked carbohydrate by weight. Maximal activity was observed at pH 2.4–5.0 and at 70°C. The β-mannosidase hydrolyzed β-1,4-linked manno-oligosaccharides of degree of polymerization (DP) 2–6 and also released mannose from polymeric ivory nut mannan and galactomannan. The Km and Vmax values for p-nitrophenyl-β-Image-mannopyranoside were 0.30 mM and 500 nkat mg−1, respectively. Hydrolysis of Image-galactose substituted manno-oligosaccharides showed that the β-mannosidase was able to cleave up to, but not beyond, a side group. An internal peptide sequence of 15 amino acids was highly similar to that of an Aspergillus aculeatus β-mannosidase belonging to family 2 of glycosyl hydrolases.
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| 8. |
- Mikkonen, K. S., et al.
(författare)
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Glucomannan composite films with cellulose nanowhiskers
- 2010
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Ingår i: Cellulose. - : Springer Science and Business Media LLC. - 0969-0239 .- 1572-882X. ; 17:1, s. 69-81
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Tidskriftsartikel (refereegranskat)abstract
- Spruce galactoglucomannans (GGM) and konjac glucomannan (KGM) were mixed with cellulose nanowhiskers (CNW) to form composite films. Remarkable effects of CNW on the appearance of the films were detected when viewed with regular and polarizing optical microscopes and with a scanning electron microscope. Addition of CNW to KGM-based films induced the formation of fiberlike structures with lengths of several millimeters. In GGM-based films, rodlike structures with lengths of several tens of micrometers were formed. The degree of crystallinity of mannan in the plasticized KGM-based films increased slightly when CNW were added, from 25 to 30%. The tensile strength of the KGM-based films not containing glycerol increased with increasing CNW content from 57 to 74 MPa, but that of glycerol-plasticized KGM and GGM films was not affected. Interestingly, the notable differences in the film structure did not appear to be related to the thermal properties of the films.
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| 9. |
- Mikkonen, Krisi S., et al.
(författare)
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Mannan-cellulose nanocomposites
- 2008
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Ingår i: Abstracts of Papers of the American Chemical Society. - 0065-7727. ; 235:228
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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| 11. |
- Palonen, H, et al.
(författare)
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Adsorption of Trichoderma reesei CBH I and EG II and their catalytic domains on steam pretreated softwood and isolated lignin
- 2004
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Ingår i: Journal of Biotechnology. - : Elsevier BV. - 1873-4863 .- 0168-1656. ; 107:1, s. 65-72
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Tidskriftsartikel (refereegranskat)abstract
- The presence of lignin has shown to play an important role in the enzymatic degradation of softwood. The adsorption of enzymes, and their constituent functional domains on the lignocellulosic material is of key importance to fundamental knowledge of enzymatic hydrolysis. In this study, we compared the adsorption of two purified cellulases from Trichoderma reesei, CBH I (Cel7A) and EG II (Cel5A) and their catalytic domains on steam pretreated softwood (SPS) and lignin using tritium labeled enzymes. Both CBH I and its catalytic domain exhibited a higher affinity to SPS than EG Il or its catalytic domain. Removal of cellulose binding domain decreased markedly the binding efficiency. Significant amounts of CBH I and EG 11 also bound to isolated lignin. Surprisingly, the catalytic domains of the two enzymes of T reesei differed essentially in the adsorption to isolated lignin. The catalytic domain of EG II was able to adsorb to alkaline isolated lignin with a high affinity, whereas the catalytic domain of CBH I did not adsorb to any of the lignins, tested. The results indicate that the cellulose binding domain has a significant role in the unspecific binding of cellulases to lignin. (C) 2003 Elsevier B.V. All rights reserved.
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| 12. |
- Parikka, K., et al.
(författare)
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Thermally stable hydrogels from enzymatically oxidized polysaccharides
- 2012
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Ingår i: Food Hydrocolloids. - : Elsevier. - 0268-005X .- 1873-7137. ; 26:1, s. 212-220
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Tidskriftsartikel (refereegranskat)abstract
- Polysaccharides guar galactomannan (guar gum), locust bean galactomannan (locust bean gum) and tamarind galactoxyloglucan were selectively oxidized by galactose oxidase. The degrees of oxidation of the products were 18-28% for guar galactomannan, 10-16% for locust bean galactomannan and 12-14% for tamarind galactoxyloglucan, calculated from the ratio of oxidized galactose units and total carbohydrates. The rheological properties of the unoxidized and oxidized polysaccharide solutions were investigated by determining their viscosities, storage and loss moduli, and temperature dependence of moduli from 20 °C to 90 °C. All the studied oxidized polysaccharides formed hydrogels throughout the entire temperature range. Concentration (0.2-1% w/v) and degree of oxidation had an effect on the gel formation. The oxidized galactomannans formed stable gels already in low concentrations, such as 0.2-0.4% w/v, while oxidized galactoxyloglucan required a concentration of 0.8% w/v to be stable up to 90 °C. The oxidized polysaccharide hydrogels are highly potential materials for food and medical applications requiring thermal stability.
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| 13. |
- Schicho, Philipp M., et al.
(författare)
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Robust approach to thermal resummation : Standard Model meets a singlet
- 2021
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Ingår i: Journal of High Energy Physics (JHEP). - : Springer Nature. - 1126-6708 .- 1029-8479. ; :6
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Tidskriftsartikel (refereegranskat)abstract
- Perturbation theory alone fails to describe thermodynamics of the electroweak phase transition. We review a technique combining perturbative and non-perturbative methods to overcome this challenge. Accordingly, the principal theme is a tutorial of high-temperature dimensional reduction. We present an explicit derivation with a real singlet scalar and compute the thermal effective potential at two-loop order. In particular, we detail the dimensional reduction for a real-singlet extended Standard Model. The resulting effective theory will impact future non-perturbative studies based on lattice simulations as well as purely perturbative investigations.
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| 15. |
- Stevanic, J. S., et al.
(författare)
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Bacterial Nanocellulose-Reinforced Arabinoxylan Films MELL TE, 1964, V19, P247
- 2011
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Ingår i: Journal of Applied Polymer Science. - : Wiley. - 1097-4628 .- 0021-8995. ; 122:2, s. 1030-1039
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Tidskriftsartikel (refereegranskat)abstract
- There is an increasing interest in substituting today's films for food packaging applications with films based on renewable resources. For this purpose, rye arabinoxylans, unmodified and enzymatically debranched, were studied for the preparation of neat films and composite films reinforced with bacterial cellulose (BC). Mixing in a homogenizer produced optically transparent, uniform films. Physical and mechanical characteristics of such films are here reported. Debranching of the arabinoxylan caused an increase in its crystallinity of 20%. Debranching as well as reinforcement with BC resulted in a decrease of the moisture sorption of the films. The debranching also resulted in a reduced breaking strain while the reinforcement with BC increased stiffness and strength of the films. (C) 2011 Wiley Periodicals, Inc. J Appl Polym Sci 122: 1030-1039, 2011
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| 17. |
- Wang, W. J., et al.
(författare)
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Biochemical and Structural Characterization of a Five-domain GH115-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40(T)
- 2016
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 291:27, s. 14120-14133
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Tidskriftsartikel (refereegranskat)abstract
- Glucuronic acid (GlcAp) and/or methylglucuronic acid (MeGlcAp) decorate the major forms of xylan in hardwood and coniferous softwoods as well as many cereal grains. Accordingly, the complete utilization of glucuronoxylans or conversion to sugar precursors requires the action of main chain xylanases as well as -glucuronidases that release the - (12)-linked (Me)GlcAp side groups. Herein, a family GH115 enzymefrom the marine bacterium Saccharophagus degradans 2-40(T), SdeAgu115A, demonstrated activity toward glucuronoxylan and oligomers thereof with preference toward MeGlcAp linked to internal xylopyranosyl residues. Unique biochemical characteristics of NaCl activation were also observed. The crystal structure of SdeAgu115A revealed a five-domain architecture, with an additional insertion C+ domain that had significant impact on the domain arrangement of SdeAgu115A monomer and its dimerization. The participation of domain C+ in substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp-335, the catalytic essentiality of Glu-216 was revealed by site-specific mutagenesis. A primary sequence analysis suggested that the SdeAgu115A architecture is shared by more than half of GH115 members, thus defining a distinct archetype for GH115 enzymes.
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