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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||endo-1,4-β-Mannanase|
High purity Mannopentaose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
Pedersen, H. L., Fangel, J. U., McCleary, B., Ruzanski, C., Rydahl, M. G., Ralet, M. C., Farkas, V., Von Schantz, L., Marcus, S. E., Andersen, M.C. F., Field, R., Ohlin, M., Knox, J. P., Clausen, M. H. & Willats, W. G. T. (2012). Journal of Biological Chemistry, 287(47), 39429-39438.
Microarrays are powerful tools for high throughput analysis, and hundreds or thousands of molecular interactions can be assessed simultaneously using very small amounts of analytes. Nucleotide microarrays are well established in plant research, but carbohydrate microarrays are much less established, and one reason for this is a lack of suitable glycans with which to populate arrays. Polysaccharide microarrays are relatively easy to produce because of the ease of immobilizing large polymers noncovalently onto a variety of microarray surfaces, but they lack analytical resolution because polysaccharides often contain multiple distinct carbohydrate substructures. Microarrays of defined oligosaccharides potentially overcome this problem but are harder to produce because oligosaccharides usually require coupling prior to immobilization. We have assembled a library of well characterized plant oligosaccharides produced either by partial hydrolysis from polysaccharides or by de novo chemical synthesis. Once coupled to protein, these neoglycoconjugates are versatile reagents that can be printed as microarrays onto a variety of slide types and membranes. We show that these microarrays are suitable for the high throughput characterization of the recognition capabilities of monoclonal antibodies, carbohydrate-binding modules, and other oligosaccharide-binding proteins of biological significance and also that they have potential for the characterization of carbohydrate-active enzymes.Hide Abstract
Rahmani, N., Kashiwagi, N., Lee, J., Niimi-Nakamura, S., Matsumoto, H., Kahar, P., Lisdiyanti, P., Yopi, Prasetya, B., Ogino, C. & Kondo, A. (2017). AMB Express, 7(1), 100.
Mannan endo-1,4-&beta-mannosidase (commonly known as &beta-mannanase) catalyzes a random cleavage of the &beta-D-1,4-mannopyranosyl linkage in mannan polymers. The enzyme has been utilized in biofuel production from lignocellulose biomass, as well as in production of mannooligosaccharides (MOS) for applications in feed and food industries. We aimed to obtain a β-mannanase, for such mannan polymer utilization, from actinomycetes strains isolated in Indonesia. Strains exhibiting high mannanase activity were screened, and one strain belonging to the genus Kitasatospora was selected. We obtained a &beta-mannanase from this strain, and an amino acid sequence of this Kitasatospora &beta-mannanase showed a 58-71% similarity with the amino acid sequences of Streptomyces &beta-mannanases. The Kitasatospora &beta-mannanase showed a significant level of activity (944 U/mg) against locust bean gum (0.5% w/v) and a potential for oligosaccharide production from various mannan polymers. The &beta-mannanase might be beneficial particularly in the enzymatic production of MOS for applications of mannan utilization.Hide Abstract
Pranovich, A., Holmbom, B. & Willför, S. (2016). Journal of Wood Chemistry and Technology, 36(2), 140-156.
In order to preserve the polymeric structure and the acetylation degree of extracted galactoglucomannans and, at the same time, achieve high yield, ground spruce wood was subjected to a series of sequential two-stage extractions with an Accelerated Solvent Extraction (ASE) apparatus using plain water at 170 deg;C. The total combined extraction time was one hour in all the extractions. The total yield of the dissolved material after 1 h extraction was almost the same, about 25% of the wood, irrespective of the time ratios between the first and the second extractions. The yield of hemicellulose high polymers with the weight average molar mass of 8-10 kDa during the first extraction had a maximum at 20 min extraction time, amounting to about 7% on dry wood basis, and comprising about half of the total extract. Along with the progress of the extraction, the molar mass of the hemicelluloses decreased and hemicellulose-derived low polymers with the weight average molar mass of 6-2 kDa became dominating. The extracted substances were fractionated, mainly according to their molar mass, by sequential precipitation with ethanol, acetone, and methyl tert-butyl ether (MTBE). The hemicelluloses with some amount of pectins comprised 83-90% of the precipitated polymeric material and the content of galactoglucomannans was about 80%.Hide Abstract
Wang, C., Zhang, J., Wang, Y., Niu, C., Ma, R., Wang, Y., Bai, Y., Luo, H. & Yao, B. (2016). Food Chemistry, 197, 474-481.
Acidophilic β-mannanases have been attracting much attention due to their excellent activity under extreme acidic conditions and significant industrial applications. In this study, a β-mannanase gene of glycoside hydrolase family 5, man5A, was cloned from Gloeophyllum trabeum CBS900.73, and successfully expressed in Pichia pastoris. Purified recombinant Man5A was acidophilic with a pH optimum of 2.5 and exhibited great pH adaptability and stability (>80% activity over pH 2.0-6.0 and pH 2.0-10.0, respectively). It had a high specific activity (1356 U/mg) against locust bean gum, was able to degrade galactomannan and glucomannan in a classical four-site binding mode, and catalyzed the transglycosylation of mannotetrose to mannooligosaccharides with higher degree of polymerization. Besides, it had great resistance to pepsin and trypsin and digested corn-soybean meal based diet in a comparable way with a commercial β-mannanase under the simulated gastrointestinal conditions of pigs. This acidophilic β-mannanase represents a valuable candidate for wide use in various industries, especially in the feed.Hide Abstract
von Freiesleben, P., Spodsberg, N., Blicher, T. H., Anderson, L., Jørgensen, H., Stålbrand, H., Meyer, A. S. & Krogh, K. B. (2016). Enzyme and Microbial Technology, 83, 68-77.
The activity and substrate degradation pattern of a novel Aspergillus nidulans GH26 endo-β-mannanase (AnMan26A) was investigated using two galactomannan substrates with varying amounts of galactopyranosyl residues. The AnMan26A was characterized in parallel with the GH26 endomannanase from Podospora anserina (PaMan26A) and three GH5 endomannanases from A. nidulans and Trichoderma reesei (AnMan5A, AnMan5C and TrMan5A). The initial rates and the maximal degree of enzymatically catalyzed conversion of locust bean gum and guar gum galactomannans were determined. The hydrolysis product profile at maximal degree of conversion was determined using DNA sequencer-Assisted Saccharide analysis in High throughput (DASH). This is the first reported use of this method for analyzing galactomannooligosaccharides. AnMan26A and PaMan26A were found to have a novel substrate degradation pattern on the two galactomannan substrates. On the highly substituted guar gum AnMan26A and PaMan26A reached 35-40% as their maximal degree of conversion whereas the three tested GH5 endomannanases only reached 8-10% as their maximal degree of conversion. α-Galactosyl-mannose was identified as the dominant degradation product resulting from AnMan26A and PaMan26A action on guar gum, strongly indicating that these two enzymes can accommodate galactopyranosyl residues in the -1 and in the +1 subsite. The degradation of α-64-63-di-galactosyl-mannopentaose by AnMan26A revealed accommodation of galactopyranosyl residues in the -2, -1 and +1 subsite of the enzyme. Accommodation of galactopyranosyl residues in subsites -2 and +1 has not been observed for other characterized endomannanases to date. Docking analysis of galactomannooligosaccharides in available crystal structures and homology models supported the conclusions drawn from the experimental results. This newly discovered diversity of substrate degradation patterns demonstrates an expanded functionality of fungal endomannanases, than hitherto reported.Hide Abstract
Rittenauer, M., Kolesnik, L., Gastl, M. & Becker, T. (2016). Food Hydrocolloids, 56, 50-57.
Starch characteristics influence the gelatinization process, which is an important prerequisite for the saccharification required in many industrial processes. In order to determine these characteristics in barley malt, an adapted purification procedure allowing to preserve the native starch composition and simultaneously segregating the amylolytic enzymes which were formed during the germination is indispensable. Therefore, this research aimed to develop a method based on a combination of dry milling, micro-sieving and density gradient centrifugation. The impact on the starch characteristics was evaluated for three germinated barley varieties. The purified starches showed starch contents greater than 90% and proteins contents less than 0.4%. Yields ranged from 40.3 to 48.6%, depending on the variety. Considering the starch properties, the amylose/amylopectin ratio was not modified during the purification. The circularity of the granules as well as the ratio of A- and B-type granules remained constant. The particle size distribution of A-granules was not shifted, B-granules with a specific diameter of 5-10 µm were slightly reduced in dependency of the native granule composition. The highest impact could be observed on the amylolytic enzymes, which were completely segregated regardless of their initial value. The standard deviation of repeatability was less than 5%, except for the determination of B-type particle size distribution (7%). The newly developed procedure supplements existing isolation methods of unmalted grains by enabling the purification of germinated barley in a reproducible manner, without altering the native starch properties and by providing pure starch free of amylolytic activity.Hide Abstract
Zang, H., Xie, S., Wu, H., Wang, W., Shao, X., Wu, L., Rajer, F. U. & Gao, X. (2015). Enzyme and microbial technology, 78, 1-9.
A novel thermostable mannanase from a newly isolated Bacillus pumilus GBSW19 has been identified, expressed, purified and characterized. The enzyme shows a structure comprising a 28 amino acid signal peptide, a glycoside hydrolase family 5 (GH5) catalytic domain and no carbohydrate-binding module. The recombinant mannanase has molecular weight of 45 kDa with an optimal pH around 6.5 and is stable in the range from pH 5-11. Meanwhile, the optimal temperature is around 65°C, and it retains 50% relative activity at 60°C for 12 h. In addition, the purified enzyme can be activated by several ions and organic solvents and is resistant to detergents. Bpman5 can efficiently convert locus bean gum to mainly M2, M3 and M5, and hydrolyze manno-oligosaccharides with a minimum DP of 3. Further exploration of the optimum condition using HPLC to prepare oligosaccharides from locust bean gum was obtained as 10 mg/ml locust bean gum incubated with 10 U/mg enzyme at 50°C for 24 h. By using this enzyme, locust bean gum can be utilized to generate high value-added oligosaccharides with a DP of 2-6.Hide Abstract
Yu, S., Li, Z., Wang, Y., Chen, W., Fu, L., Tang, W., Chen, C., Liu, Y., Zhang, X. & Ma, L. (2015). Biotechnology Letters, 37(9), 1853-1859.
Objectives: A novel, high-level expression, thermostable mannan endo-1,4-β-mannosidase is urgently needed for industrial applications. Results: The mannan endo-1,4-β-mannosidase gene (MAN) from Aspergillus niger CBS 513.88 was optimized based on the codon usage bias in Pichia pastoris and synthesized by overlapping PCR to produce MAN-P. It was expressed in P. pastoris GS115 from a constitutive expression vector pHBM-905 M. MAN-P reached 594 mg/l in shake-flasks after 192 h induction. On production in a 5 l fermenter, the yield of MAN-P reached ~3.5 mg/ml and the enzyme activity was 1612 U/ml. The enzyme exhibited a maximum activity of 3049 U/ml at 80°C and retained 60 % enzyme activity at 80°C for 2 h. The pH optimum was 4.5 and the enzyme was stable over the pH range 1.5-11. Conclusion: The thermostability of MAN-P is higher than other known fungal mannanases and the expression and thermophilic properties make MAN-P useful for industrial applications.Hide Abstract
Navidshad, B., Liang, J. B., Jahromi, M. F., Akhlaghi, A. & Abdullah, N. (2015). Italian Journal of Animal Science, 14(1), 3452.
The present study was conducted to determine the effect of a yeast cell wall extract (Bio-Mos) and palm kernel expeller (PKE) on the performance, nutrient digestibility, and ileal bacteria population of broiler chickens. A total of 60 1-d-old male broiler chicks (Cobb 500) were fed one of the 3 isonitrogenous and isocaloric diet including a control diet, or a control diet supplemented with 2 g/kg Bio-Mos (1-42 d), and for the third group, the control diet at 1-28 d following a diet containing 200 g/kg of an enzymatically-treated PKE at 29-42 d. The weight gains of birds fed the PKE containing diet (96.17 g/d) were less than other groups (109.10 and 104.42 g/d for the Bio-Mos and control diet, respectively) (P<0.05). Dietary inclusion of PKE increased bird’s feed intake (214.45 g/d) and feed conversion ratio (FCR) (2.23) than the Bio-Mos diet (194.87 and 1.79 g/d for feed intake and FCR, respectively) (P<0.05). The PKE diet had lower digestibility coefficients for dry matter (83.37%), ash and crude protein (78.63%) than the PKE free diets (P<0.05). As a ratio of the ileal total bacteria, there were no differences in the ileal population of Lactobacilli and Enterococcus genus or Enterobacteriaceae among the experimental groups (P>0.05), but the birds fed PKE or Bio-Mos containing diets had a lower population of Escherichia colithan the control group (P<0.05). The results showed that PKE potentially has a prebiotic property for chicken; however, a 200 g/kg dietary inclusion rate of PKE is not commercially recommendable because of its negative effects on the nutrients digestibility.Hide Abstract
Hori, K., Kawabata, Y., Nakazawa, Y., Nishizawa, M. & Toeda, K. (2014). Food Science and Technology Research, 20(6), 1261-1265.
A β-1,4-mannanase producing bacterium was isolated from soil collected in Akita Prefecture, Japan. The bacterium was identified as Paenibacillus polymyxa KT551 and was shown to produce a novel β-1,4-mannanase. The novelty of the enzyme was established by its N-terminal amino acid sequence, molecular weight and isoelectric point. The isolated β-1,4-mannanase showed activity against mannotetraose, mannopentaose and mannohexaose to produce mannobiose, mannotriose and mannotetraose. However, the enzyme exhibited no activity against mannobiose and mannotriose. Moreover, the crude enzyme preparation of the bacterium had no or minimal β-mannosidase or α-galactosidase activity. Therefore, the enzyme preparation from P. polymyxa KT551 holds potential for the efficient production of mannooligosaccharides from natural resources of galactomannans.Hide Abstract
Lu, H., Luo, H., Shi, P., Huang, H., Meng, K., Yang, P. & Yao, B. (2014). Applied Microbiology and Biotechnology, 98(5), 2155-2163.
The gene man5XZ3 from Aspergillus nidulans XZ3 encodes a multimodular β-mannanase of glycoside hydrolase family 5 that consists of a family 1 carbohydrate-binding module (CBM1), a Thr/Ser-rich linker region, and a catalytic domain. Recombinant Man5XZ3 and its two truncated derivatives, Man5ΔCBM (removing the CBM1) and Man5ΔCL (removing both the CBM1 and linker region), were produced in Pichia pastoris and showed significant variance in the secondary structure. The three enzymes had similar biochemical properties, such as optimal pH and temperature (pH 5.0 and 80°C) and excellent pH stability at pH 4.0–10.0. Removal of the CBM1 alone could improve the thermostability of Man5XZ3, but further removal of the linker region resulted in worse thermostability. Man5XZ3 retained greater enzyme activity in the presence of an organic solvent (acetone), two detergents (SDS and Triton X-100), and a chaotropic agent (urea) compared with Man5ΔCBM and Man5ΔCL. This study provides an excellent β-mannanase candidate favorable for various industries and primarily demonstrates the relationship between enzyme structure and function.Hide Abstract
González-Muñoz, M. J., Rivas, S., Santos, V. & Parajó, J. C. (2013). Journal of Membrane Science, 428, 281-289.
Hemicelluloses of Pinus pinaster wood were selectively separated from cellulose and lignin by reaction with hot, compressed water (autohydrolysis) under optimized conditions. The reaction liquor contained polymeric or oligomeric hemicellulose saccharides (POHS, accounting jointly for 69.6% of the dissolved wood fraction), followed by monosaccharides (accounting for 20.0% of the non-volatile compounds), and non-saccharide compounds. For concentration, purification and fractionation purposes, liquors from hydrothermal processing were subjected to consecutive steps of diafiltration and concentration using membranes of 10, 5, 3, 1 and 0.3 kDa molar mass cut-off. Samples from selected process streams were characterized by chromatographic and spectrometric methods. The experimental results provided information on the separation and refining effects achieved by the various membrane processing steps, which affect the technological properties of products.Hide Abstract
Li, S. H., Zhu, M. P. & Li, T. P. (2011). Advanced Materials Research, 183, 447-451.
The α-galactosidase from rice cleaved not only α-D-galactosyl residues from the non-reducing end of substrates such as melibiose, raffinose and stachyose, but also liberated the terminal galactosyl residues attached O-6 position of the reducing-end mannosyl residue in mannobiose and mannotriose. In addition, the enzyme tore off the stubbed galactosyl residues attached inner-mannosyl residues in mannopentaose. It also could catalyze efficient degalactosylation of galactomannans, such as guar gum and locust bean gum.Hide Abstract
Cai, H., Shi, P., Luo, H., Bai, Y., Huang, H., Yang, P. & Yao, B. (2011). Journal of Bioscience and Bioengineering, 112(6), 551-557.
The β-mannanase gene, man5C1, was cloned from Penicillium pinophilum C1, a strain isolated from the acidic wastewater of a tin mine in Yunnan, China, and expressed in Pichia pastoris. The sequence analysis displayed the gene consists of a 1221-bp open reading frame encoding a protein of 406 amino acids (Man5C1). The deduced amino acid sequence of Man5C1 showed the highest homology of 57.8% (identity) with a characterized β-mannanase from Aspergillus aculeatus belonging to glycoside hydrolase family 5. The purified rMan5C1 had a high specific activity of 1035 U mg-1 towards locust bean gum (LBG) and showed highest activity at pH 4.0 and 70°C. rMan5C1 was adaptable to a wide range of acidity, retaining > 60% of its maximum activity at pH 3.0–7.0. The enzyme was stable over a broad pH range (3.0 to 10.0) and exhibited good thermostability at 50°C. The Km and Vmax values were 5.6 and 4.8 mg mL-1, and 2785 and 1608 μmol min-1 mg-1, respectively, when LBG and konjac flour were used as substrates. The enzyme had strong resistance to most metal ions and proteases (pepsin and trypsin), and released 8.96 mg g-1 reducing sugars from LBG in the simulated gastric fluid. All these favorable properties make rMan5C1 a promising candidate for use in animal feed.Hide Abstract
Schröder, R., Wegrzyn, T. F., Sharma, N. N. & Atkinson, R. G. (2006). Planta, 224(5), 1091-1102.
Mannan transglycosylases are cell wall enzymes able to transfer part of the mannan polysaccharide backbone to mannan-derived oligosaccharides (Schröder et al. in Planta 219:590–600, 2004). Mannan transglycosylase activity was purified to near homogeneity from ripe tomato fruit. N-terminal sequencing showed that the dominant band seen on SDS-PAGE was identical to LeMAN4a, a hydrolytic endo-β-mannanase found in ripe tomato fruit (Bewley et al. in J Exp Bot 51:529–538, 2000). Recombinant LeMAN4a protein expressed in Escherichia coli exhibited both mannan hydrolase and mannan transglycosylase activity. Western analysis of ripe tomato fruit tissue using an antibody raised against tomato seed endo-β-mannanase revealed four isoforms present after 2D-gel electrophoresis in the pH range 6–11. On separation by preparative liquid isoelectric focussing, these native isoforms exhibited different preferences for transglycosylation and hydrolysis. These results demonstrate that endo-β-mannanase has two activities: it can either hydrolyse mannan polysaccharides, or in the presence of mannan-derived oligosaccharides, carry out a transglycosylation reaction. We therefore propose that endo-β-mannanase should be renamed mannan transglycosylase/hydrolase, in accordance with the nomenclature established for xyloglucan endotransglucosylase/hydrolase. The role of endo-acting mannanases in modifying the structure of plant cell walls during cell expansion, seed germination and fruit ripening may need to be reinterpreted in light of their potential action as transglycosylating or hydrolysing enzymes.Hide Abstract
Tunnicliffe, R. B., Bolam, D. N., Pell, G., Gilbert, H. J. & Williamson, M. P. (2005). Journal of Molecular Biology, 347(2), 287-296.
Enzymes that digest plant cell wall polysaccharides generally contain non-catalytic, carbohydrate-binding modules (CBMs) that function by attaching the enzyme to the substrate, potentiating catalytic activity. Here, we present the first structure of a family 35 CBM, derived from the Cellvibrio japonicus β-1,4-mannanase Man5C. The NMR structure has been determined for both the free protein and the protein bound to mannopentaose. The data show that the protein displays a typical β-jelly-roll fold. Ligand binding is not located on the concave surface of the protein, as occurs in many CBMs that display the jelly-roll fold, but is formed by the loops that link the two β-sheets of the protein, similar to family 6 CBMs. In contrast to the majority of CBMs, which are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. The curvature of the binding site and the narrow binding cleft are likely to be the main determinants of binding specificity. The predicted solvent exposure of O6 at several subsites provides an explanation for the observed accommodation of decorated mannans. Two of the key aromatic residues in Man5C-CBM35 that interact with mannopentaose are conserved in mannanase-derived CBM35s, which will guide specificity predictions based on the primary sequence of proteins in this CBM family.Hide Abstract
Hogg, D., Pell, G., Dupree, P., Goubet, F., Martin-Orue, S., Armand, S. & Gilbert, H. (2003). Biochem. J, 371(3), 1027-1043.
β-1,4-Mannanases (mannanases), which hydrolyse mannans and glucomannans, are located in glycoside hydrolase families (GHs) 5 and 26. To investigate whether there are fundamental differences in the molecular architecture and biochemical properties of GH5 and GH26 mannanases, four genes encoding these enzymes were isolated from Cellvibrio japonicus and the encoded glycoside hydrolases were characterized. The four genes, man5A, man5B, man5C and man26B, encode the mannanases Man5A, Man5B, Man5C and Man26B, respectively. Man26B consists of an N-terminal signal peptide linked via an extended serine-rich region to a GH26 catalytic domain. Man5A, Man5B and Man5C contain GH5 catalytic domains and non-catalytic carbohydrate-binding modules (CBMs) belonging to families 2a, 5 and 10; Man5C in addition contains a module defined as X4 of unknown function. The family 10 and 2a CBMs bound to crystalline cellulose and ivory nut crystalline mannan, displaying very similar properties to the corresponding family 10 and 2a CBMs from Cellvibrio cellulases and xylanases. CBM5 bound weakly to these crystalline polysaccharides. The catalytic domains of Man5A, Man5B and Man26B hydrolysed galactomannan and glucomannan, but displayed no activity against crystalline mannan or cellulosic substrates. Although Man5C was less active against glucomannan and galactomannan than the other mannanases, it did attack crystalline ivory nut mannan. All the enzymes exhibited classic endo-activity producing a mixture of oligosaccharides during the initial phase of the reaction, although their mode of action against manno-oligosaccharides and glucomannan indicated differences in the topology of the respective substrate-binding sites. This report points to a different role for GH5 and GH26 mannanases from C. japonicus. We propose that as the GH5 enzymes contain CBMs that bind crystalline polysaccharides, these enzymes are likely to target mannans that are integral to the plant cell wall, while GH26 mannanases, which lack CBMs and rapidly release mannose from polysaccharides and oligosaccharides, target the storage polysaccharide galactomannan and manno-oligosaccharides.Hide Abstract
Hägglund, P., Eriksson, T., Collén, A., Nerinckx, W., Claeyssens, M. & Stålbrand, H. (2003). Journal of Biotechnology, 101(1), 37-48.
Endo-β-1,4-D-mannanases (β-mannanase; EC 184.108.40.206) are endohydrolases that participate in the degradation of hemicellulose, which is closely associated with cellulose in plant cell walls. The β-mannanase from Trichoderma reesei (Man5A) is composed of an N-terminal catalytic module and a C-terminal carbohydrate-binding module (CBM). In order to study the properties of the CBM, a construct encoding a mutant of Man5A lacking the part encoding the CBM (Man5AΔCBM), was expressed in T. reesei under the regulation of the Aspergillus nidulans gpdA promoter. The wild-type enzyme was expressed in the same way and both proteins were purified to electrophoretic homogeneity using ion-exchange chromatography. Both enzymes hydrolysed mannopentaose, soluble locust bean gum galactomannan and insoluble ivory nut mannan with similar rates. With a mannan/cellulose complex, however, the deletion mutant lacking the CBM showed a significant decrease in hydrolysis. Binding experiments using activity detection of Man5A and Man5AΔCBM suggests that the CBM binds to cellulose but not to mannan. Moreover, the binding of Man5A to cellulose was compared with that of an endoglucanase (Cel7B) from T. reesei.Hide Abstract
Pettolino, F. A., Hoogenraad, N. J., Ferguson, C., Bacic, A., Johnson, E. & Stone, B. A. (2001). Planta, 214(2), 235-242.
Galactomannan was coupled to a protein carrier for the preparation of monoclonal antibodies. The monoclonal antibodies generated bound to galactomannans from different sources as well as to glucomannan and galactoglucomannan. One monoclonal antibody, BGM C6, was characterised and found to be specific for (1→4)-β-linked mannopyranosyl residues; it had a binding affinity estimated at 1×10-6) M for the (1→4)-β-linked mannohexaose. BGM C6 was used in immunogold labelling studies to locate galactomannans in the endosperm walls of normal coconuts (Cocos nucifera L.) and those of the mutant makapuno at two different developmental stages. The pattern and intensity of antibody labelling varied for each type of coconut at the mature and immature stages, indicating differences in the galactomannan composition of the endosperm walls.Hide Abstract
Nattorp, A., Graf, M., Spühler, C. & Renken, A. (1999). Industrial & Engineering Chemistry Research, 38(8), 2919-2926.
The kinetics for homogeneous hydrolysis of mannan is studied in a batch reactor at temperatures from 160 to 220°C. A formate buffer ensures a pH of 3.8−4.0, measured at 25°C. Samples are analyzed for oligosaccharides up to a degree of polymerization of 6 and also for the total amount of mannose after acid hydrolysis. A mathematical model with two reactions (1, random hydrolysis of the glucosidic bonds; 2, degradation of the reducing end of the molecule) describes accurately the time course of oligosaccharides. Optimized rate constants follow closely an Arrhenius relationship, with the degradation having a higher activation energy (140 kJ/mol) than the hydrolysis (113 kJ/mol). The mathematical model has the advantage that production of small molecules is independent of the initial chain-length distribution as long as the average initial chain length is some 5 times longer than the largest species measured. It can be applied to first-order depolymerization of other linear polymers with one link type in order to determine reaction rate constants or make predictions about molecular weight distribution on the base of known reaction rate constants.Hide Abstract