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Xyloglucan (Tamarind)

Xyloglucan Tamarind P-XYGLN
Product code: P-XYGLN

3 g

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Content: 3 g
Shipping Temperature: Ambient
Storage Temperature: Ambient
Physical Form: Powder
Stability: > 2 years under recommended storage conditions
CAS Number: 37294-28-3
Source: Tamarind seed
Purity: > 95%
Viscosity: 142 cSt at 1% Solution
Monosaccharides (%): Xylose: Glucose: Galactose: Arabinose: Other sugars = 34: 45: 17: 2: 2
Main Chain Glycosidic Linkage: β-1,4, α-1,6 and β-1,6
Substrate For (Enzyme): endo-Cellulase, Xyloglucanase

High purity Xyloglucan (Tamarind) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

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Data Sheet

A systematic analysis of marine lysogens and proviruses.

Yi, Y., Liu, S., Hao, Y., Sun, Q., Lei, X., Wang, Y., Wang, J., Zhang, M., Tang, S., Tang, Q., Zhang, Y., Liu, X., Wang, Y., Xiao, X. & Jian, H. (2023). Nature Communications, 14(1), 6013.

Viruses are ubiquitous in the oceans, exhibiting high abundance and diversity. Here, we systematically analyze existing genomic sequences of marine prokaryotes to compile a Marine Prokaryotic Genome Dataset (MPGD, consisting of over 12,000 bacterial and archaeal genomes) and a Marine Temperate Viral Genome Dataset (MTVGD). At least 40% of the MPGD genomes contain one or more proviral sequences, indicating that they are lysogens. The MTVGD includes over 12,900 viral contigs or putative proviruses, clustered into 10,897 viral genera. We show that lysogens and proviruses are abundant in marine ecosystems, particularly in the deep sea, and marine lysogens differ from non-lysogens in multiple genomic features and growth properties. We reveal several virus-host interaction networks of potential ecological relevance, and identify proviruses that appear to be able to infect (or to be transferred between) different bacterial classes and phyla. Auxiliary metabolic genes in the MTVGD are enriched in functions related to carbohydrate metabolism. Finally, we experimentally demonstrate the impact of a prophage on the transcriptome of a representative marine Shewanella bacterium. Our work contributes to a better understanding of the ecology of marine prokaryotes and their viruses.

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The secretome of Agaricus bisporus: temporal dynamics of plant polysaccharides and lignin degradation.

Duran, K., Magnin, J., America, A. H., Peng, M., Hilgers, R., de Vries, R. P., Baars, J. J. P., Berkel, W. J. H., Kuyper, T. W. & Kabel, M. A. (2023). iScience, 26(7): 107087.

Despite substantial lignocellulose conversion during mycelial growth, previous transcriptome and proteome studies have not yet revealed how secretomes from the edible mushroom Agaricus bisporus develop and whether they modify lignin models in vitro. To clarify these aspects, A. bisporus secretomes collected throughout a 15-day industrial substrate production and from axenic lab-cultures were subjected to proteomics, and tested on polysaccharides and lignin models. Secretomes (day 6-15) comprised A. bisporus endo-acting and substituent-removing glycoside hydrolases, whereas β-xylosidase and glucosidase activities gradually decreased. Laccases appeared from day 6 onwards. From day 10 onwards, many oxidoreductases were found, with numerous multicopper oxidases (MCO), aryl alcohol oxidases (AAO), glyoxal oxidases (GLOX), a manganese peroxidase (MnP), and unspecific peroxygenases (UPO). Secretomes modified dimeric lignin models, thereby catalyzing syringylglycerol-β-guaiacyl ether (SBG) cleavage, guaiacylglycerol-β-guaiacyl ether (GBG) polymerization, and non-phenolic veratrylglycerol-β-guaiacyl ether (VBG) oxidation. We explored A. bisporus secretomes and insights obtained can help to better understand biomass valorization.

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Structures of the xyloglucans in the monocotyledon family Araceae (aroids).

Hsiung, S. Y., Li, J., Imre, B., Kao, M. R., Liao, H. C., Wang, D., Chen, C. C., Liang, P. H., Harris, P. J. & Hsieh, Y. S. (2023). Planta, 257(2), 39.

The aquatic Araceae species Lemna minor was earlier shown to have xyloglucans with a different structure from the fucogalactoxyloglucans of other non-commelinid monocotyledons. We investigated 26 Araceae species (including L. minor), from five of the seven subfamilies. All seven aquatic species examined had xyloglucans that were unusual in having one or two of three features: < 77% XXXG core motif [L. minor (Lemnoideae) and Orontium aquaticum (Orontioideae)]; no fucosylation [L. minor (Lemnoideae), Cryptocoryne aponogetonifolia, and Lagenandra ovata (Aroideae, Rheophytes clade)]; and > 14% oligosaccharide units with S or D side chains [Spirodela polyrhiza and Landoltia punctata (Lemnoideae) and Pistia stratiotes (Aroideae, Dracunculus clade)]. Orontioideae and Lemnoideae are the two most basal subfamilies, with all species being aquatic, and Aroideae is the most derived. Two terrestrial species [Dieffenbachia seguine and Spathicarpa hastifolia (Aroideae, Zantedeschia clade)] also had xyloglucans without fucose indicating this feature was not unique to aquatic species.

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Novel, acidic, and cold-adapted glycoside hydrolase family 8 endo-β-1, 4-glucanase from an Antarctic lichen-associated bacterium, Lichenicola cladoniae PAMC 26568.

Kim, J., Lee, Y. M., Byeon, S. M., Gwak, J. H., Lee, J. S., Shin, D. H. & Park, H. Y. (2022). Frontiers in Microbiology, 13.

Endo-β-1,4-glucanase is a crucial glycoside hydrolase (GH) involved in the decomposition of cellulosic materials. In this study, to discover a novel cold-adapted β-1,4-d-glucan-degrading enzyme, the gene coding for an extracellular endo-β-1,4-glucanase (GluL) from Lichenicola cladoniae PAMC 26568, an Antarctic lichen (Cladonia borealis)-associated bacterium, was identified and recombinantly expressed in Escherichia coli BL21. The GluL gene (1044-bp) encoded a non-modular polypeptide consisting of a single catalytic GH8 domain, which shared the highest sequence identity of 55% with that of an uncharacterized protein from Gluconacetobacter takamatsuzukensis (WP_182950054). The recombinant endo-β-1,4-glucanase (rGluL: 38.0 kDa) most efficiently degraded sodium carboxymethylcellulose (CMC) at pH 4.0 and 45°C, and showed approximately 23% of its maximum degradation activity even at 3°C. The biocatalytic activity of rGluL was noticeably enhanced by >1.3-fold in the presence of 1 mM Mn2+ or NaCl at concentrations between 0.1 and 0.5 M, whereas the enzyme was considerably downregulated by 1 mM Hg2+ and Fe2+ together with 5 mM N-bromosuccinimide and 0.5% sodium dodecyl sulfate. rGluL is a true endo-β-1,4-glucanase, which could preferentially decompose d-cellooligosaccharides consisting of 3 to 6 d-glucose, CMC, and barley β-glucan, without other additional glycoside hydrolase activities. The specific activity (15.1 U mg–1) and kcat/Km value (6.35 mg–1 s–1mL) of rGluL toward barley β-glucan were approximately 1.8- and 2.2-fold higher, respectively, compared to its specific activity (8.3 U mg–1) and kcat/Km value (2.83 mg–1 s–1mL) toward CMC. The enzymatic hydrolysis of CMC, d-cellotetraose, and d-cellohexaose yielded primarily d-cellobiose, accompanied by d-glucose, d-cellotriose, and d-cellotetraose. However, the cleavage of d-cellopentaose by rGluL resulted in the production of only d-cellobiose and d-cellotriose. The findings of the present study imply that rGluL is a novel, acidic, and cold-adapted GH8 endo-β-1,4-glucanase with high specific activity, which can be exploited as a promising candidate in low-temperature processes including textile and food processes.

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Elucidating the role of SlXTH5 in tomato fruit softening.

Wang, D., Lu, Q., Wang, X., Ling, H. & Huang, N. (2022). Horticultural Plant Journal, In Press.

Fruit softening in tomato (Solanum lycopersicum) is closely associated with cell wall disassembly, which is brought about through the action of a range of cell wall structure-related enzymes and other proteins such as expansins. Xyloglucan endotransglucosylase/hydrolase (XTH) (EC and/or EC has been proposed to be key player involved in xyloglucan metabolism. SlXTH5 showed the highest expression level among all SlXTHs during tomato ripening. In this study, the role of SlXTH5 involved in tomato softening was investigated in CRISPR-based knockout mutants of SlXTH5. Loss-of-function of SlXTH5 in transgenic tomato lines resulted in slightly firmer fruit pericarp, but significantly decreased their color index compared with azygous wild type (WT) control fruits. Increased paste viscosity was detected in CRISPR mutants, indicating that the activity of SlXTH5 is responsible for maintaining cell wall structural integrity. Immunocytochemistry studies were performed using the monoclonal antibody probe LM25 to examine the localization and distribution of xyloglucan in the pericarp cells of the CRISPR mutant fruits. The data indicated more xyloglucan was retained in the pericarp of CRISPR mutant fruit than in WT control fruit. This study revealed the link between SlXTH5 and xyloglucan metabolism and indicated the potential of manipulating SlXTH5 to regulate fruit softening.

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Effects of hemicelluloses on dehydrogenative polymerization of monolignols with cationic cell wall-bound peroxidase.

Lyu, Y., Suzuki, S., Nagano, H., Shigetomi, K., Tamai, Y., Tsutsumi, Y. & Uraki, Y. (2022). Carbohydrate Polymers, 301, 120305.

To elucidate the influence of polysaccharides on hardwood lignification, dehydrogenative polymerization of monolignols, coniferyl alcohol (CA) and sinapyl alcohol (SA), was attempted with recombinant cationic cell wall-bound peroxidase (rCWPO-C) and horseradish peroxidase (HRP) in measurement cells of a quartz crystal microbalance with dissipation (QCM-D). Hardwood cellulose nanofibers were anchored; hemicelluloses, xylan, partially acetylated xylan (AcXY), galactoglucomannan, and xyloglucan, and the enzymes were subsequently adsorbed onto the QCM-D sensor surface, enabling fabrication of artificial polysaccharide matrices. The largest amount of rCWPO-C is found to be adsorbed onto AcXY among all the polysaccharides, which affords the largest amount and size of spherical dehydrogenation polymers (DHPs) from both CA and SA. In contrast, no DHP and a small amount of DHPs are formed from SA and CA, respectively, by HRP catalysis in all of the polysaccharide matrices. This study demonstrates important functions of a real tree-derived peroxidase, rCWPO-C, and AcXY for hardwood lignification.

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Acetylation modification improved the physicochemical properties of xyloglucan from tamarind seeds.

Zhang, H., Zhao, T., Wu, Y., Xie, F., Xiong, Z., Song, Z., Ai, L. & Wang, G. (2022). International Journal of Biological Macromolecules, 223, 193-201.

Acetylation modification was conducted to improve the water-solubility and solution properties of xyloglucan from tamarind seeds (TSX). Three acetylated TSX with different degree of substitution (DS) were successfully prepared, and their structure and molecular parameters were investigated by FT-IR, NMR, and high-performance size exclusion chromatography (HPSEC). Further, the effects of acetylation on the thermal stability, solubility, and rheological properties of TSX were studied. Results showed that acetyl groups were mainly substituted at the O-6 position of terminal galactose with DS of 0.2, 0.47, and 0.36 for AC-2, AC-5, and AC-10, respectively. HPSEC analysis indicated that molecular weight of acetylated derivatives decreased slightly, and the solution conformation became more flexible as the DS increase. By comparing with TSX, the thermal stability, water-solubility, solution transmittance, and ζ-potential of acetylated TSX were significantly improved as the DS increase. In addition, rheological studies demonstrated that acetylation reduced the shear viscosity, but high DS of acetylation could induce the weak gelling property of TSX. In conclusion, acetylation modification could be applied to improve the physicochemical properties of TSX and promote its further application in food and pharmaceutical industries.

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Microarray-guided evaluation of the frequency, B-cell origins, and selectivity of human glycan-binding antibodies reveals new insights and novel antibodies.

Temme, J. S., Crainic, J. A., Walker, L. M., Yang, W., Tan, Z., Huang, X., & Gildersleeve, J. C. (2022). Journal of Biological Chemistry, 298(10).

The immune system produces a diverse collection of antiglycan antibodies that are critical for host defense. At present, however, we know very little about the binding properties, origins, and sequences of these antibodies because of a lack of access to a variety of defined individual antibodies. To address this challenge, we used a glycan microarray with over 800 different components to screen a panel of 516 human monoclonal antibodies that had been randomly cloned from different B-cell subsets originating from healthy human subjects. We obtained 26 antiglycan antibodies, most of which bound microbial carbohydrates. The majority of the antiglycan antibodies identified in the screen displayed selective binding for specific glycan motifs on our array and lacked polyreactivity. We found that antiglycan antibodies were about twice as likely than expected to originate from IgG+ memory B cells, whereas none were isolated from naïve, early emigrant, or immature B cells. Therefore, our results indicate that certain B-cell subsets in our panel are enriched in antiglycan antibodies, and IgG+ memory B cells may be a promising source of such antibodies. Furthermore, some of the newly identified antibodies bound glycans for which there are no reported monoclonal antibodies available, and these may be useful as research tools, diagnostics, or therapeutic agents. Overall, the results provide insight into the types and properties of antiglycan antibodies produced by the human immune system and a framework for the identification of novel antiglycan antibodies in the future.

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Duplication of horizontally acquired GH5_2 enzymes played a central role in the evolution of longhorned beetles.

Shin, N. R., Doucet, D. & Pauchet, Y. (2022). Molecular Biology and Evolution, 39(6), msac128.

The rise of functional diversity through gene duplication contributed to the adaption of organisms to various environments. Here we investigate the evolution of putative cellulases of the subfamily 2 of glycoside hydrolase family 5 (GH5_2) in the Cerambycidae (longhorned beetles), a megadiverse assemblage of mostly xylophagous beetles. Cerambycidae originally acquired GH5_2 from a bacterial donor through horizontal gene transfer (HGT), and extant species harbor multiple copies that arose from gene duplication. We ask how these digestive enzymes contributed to the ability of these beetles to feed on wood. We analyzed 113 GH5_2, including the functional characterization of 52 of them, derived from 25 species covering most subfamilies of Cerambycidae. Ancestral gene duplications led to five well-defined groups with distinct substrate specificity, allowing these beetles to break down, in addition to cellulose, polysaccharides that are abundant in plant cell walls (PCWs), namely, xyloglucan, xylan, and mannans. Resurrecting the ancestral enzyme originally acquired by HGT, we show it was a cellulase that was able to break down glucomannan and xylan. Finally, recent gene duplications further expanded the catalytic repertoire of cerambycid GH5_2, giving rise to enzymes that favor transglycosylation over hydrolysis. We suggest that HGT and gene duplication, which shaped the evolution of GH5_2, played a central role in the ability of cerambycid beetles to use a PCW-rich diet and may have contributed to their successful radiation.

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Mapping molecular recognition of β1, 3-1, 4-glucans by a surface glycan-binding protein from the human gut symbiont Bacteroides ovatus.

Correia, V. G., Trovão, F., Pinheiro, B. A., Brás, J. L., Silva, L. M., Nunes, C., Cimbra, M. A., Liu, Y., Feizi, T., Fontes, C. M. G. A., Mulloy, B., Chai, W., Carvalho, A. L. & Palma, A. S. (2021). Microbiology Spectrum, 9(3), e01826-21.

A multigene polysaccharide utilization locus (PUL) encoding enzymes and surface carbohydrate (glycan)-binding proteins (SGBPs) was recently identified in prominent members of Bacteroidetes in the human gut and characterized in Bacteroides ovatus. This PUL-encoded system specifically targets mixed-linkage β1,3-1,4-glucans, a group of diet-derived carbohydrates that promote a healthy microbiota and have potential as prebiotics. The BoSGBPMLG-A protein encoded by the BACOVA_2743 gene is a SusD-like protein that plays a key role in the PUL's specificity and functionality. Here, we perform a detailed analysis of the molecular determinants underlying carbohydrate binding by BoSGBPMLG-A, combining carbohydrate microarray technology with quantitative affinity studies and a high-resolution X-ray crystallography structure of the complex of BoSGBPMLG-A with a β1,3-1,4-nonasaccharide. We demonstrate its unique binding specificity toward β1,3-1,4-gluco-oligosaccharides, with increasing binding affinities up to the octasaccharide and dependency on the number and position of β1,3 linkages. The interaction is defined by a 41-Å-long extended binding site that accommodates the oligosaccharide in a mode distinct from that of previously described bacterial β1,3-1,4-glucan-binding proteins. In addition to the shape complementarity mediated by CH-π interactions, a complex hydrogen bonding network complemented by a high number of key ordered water molecules establishes additional specific interactions with the oligosaccharide. These support the twisted conformation of the β-glucan backbone imposed by the β1,3 linkages and explain the dependency on the oligosaccharide chain length. We propose that the specificity of the PUL conferred by BoSGBPMLG-A to import long β1,3-1,4-glucan oligosaccharides to the bacterial periplasm allows Bacteroidetes to outcompete bacteria that lack this PUL for utilization of β1,3-1,4-glucans. 

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