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Journal articles on the topic 'Cello-oligosaccharides'

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Published: 20 April 2024

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1

Bhat, K. M., A. J. Hay, M. Claeyssens, and T. M. Wood. "Study of the mode of action and site-specificity of the endo-(1→4)-β-d-glucanases of the fungus Penicillium pinophilum with normal, 1-3H-labelled, reduced and chromogenic cello-oligosaccharides." Biochemical Journal 266, no. 2 (March 1, 1990): 371–78. http://dx.doi.org/10.1042/bj2660371.

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The modes of action of the five major endo-(1→4)-beta-D-glucanases (I, II, III, IV and V) purified from Penicillium pinophilum cellulase were compared by h.p.l.c. analysis, with normal, 1-3H-labelled and reduced cello-oligosaccharides and 4-methylumbelliferyl glycosides as substrates. Significant differences were observed in the preferred site of cleavage even when substrates with the same number of glycosidic bonds were compared. Thus, although endoglucanase I was unable to attack normal cello-oligosaccharides shorter than degree of polymerization 6, it hydrolysed reduced cellopentaose to yield cellotriose and cellobi-itol, and it produced cellotriose and 4-methylumbelliferyl glucoside from 4-methylumbelliferyl cellotetraoside. Endoglucanase IV hydrolysed [1-3H]cellotriose but did not attack either cellotri-itol or 4-methylumbelliferyl cellobioside. These and other anomalous results indicated clearly that modification of the reducing glycosyl residue on the cello-oligosaccharides induces in an apparent change in the mode of action of the endoglucanases. It is suggested that, although cello-oligosaccharide derivatives are useful for differentiating and classifying endoglucanases, conclusions on the mechanism of cellulase action resulting from these measurements should be treated cautiously. Unequivocal information on the mode of endoglucanase action on cello-oligosaccharides was obtained with radiolabelled cello-oligosaccharides of degree of polymerization 3 to 5. Indications that transglycosylation was a property of the endoglucanases were particularly evident with the 4-methylumbelliferyl cello-oligosaccharides. Turnover numbers for hydrolysis of the umbelliferyl cello-oligosaccharides were calculated, and these, along with the other analytical data collected on the products of hydrolysis of the normal, reduced and radiolabelled cello-oligosaccharides, suggested that the various endoglucanases had different roles to play in the overall hydrolysis of cellulose to sugars small enough to be transported through the cell membrane.

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2

NAKATSUBO, Fumiaki. "Chemical Synthesis of Cello-Oligosaccharides." Kobunshi 46, no. 10 (1997): 743–44. http://dx.doi.org/10.1295/kobunshi.46.743.

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3

Kamitakahara, Hiroshi, Fumiaki Nakatsubo, and Dieter Klemm. "ChemInform Abstract: Synthesis of Methylated Cello-oligosaccharides: Synthesis Strategy for Blockwise Methylated Cello-oligosaccharides." ChemInform 41, no. 29 (June 24, 2010): no. http://dx.doi.org/10.1002/chin.201029264.

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4

Chen, Pengru, Abhijit Shrotri, and Atsushi Fukuoka. "Unraveling the hydrolysis of β-1,4-glycosidic bonds in cello-oligosaccharides over carbon catalysts." Catalysis Science & Technology 10, no. 14 (2020): 4593–601. http://dx.doi.org/10.1039/d0cy00783h.

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Larger cello-oligosaccharides undergo faster hydrolysis over carbon catalysts. This is attributed to reduction in activation energy caused by conformational change in the structure of oligosaccharides as they adsorb within the micropores of carbon.

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5

Chu, Qiulu, Xin Li, Yong Xu, Zhenzhen Wang, Jing Huang, Shiyuan Yu, and Qiang Yong. "Functional cello-oligosaccharides production from the corncob residues of xylo-oligosaccharides manufacture." Process Biochemistry 49, no. 8 (August 2014): 1217–22. http://dx.doi.org/10.1016/j.procbio.2014.05.007.

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6

Francis, Isolde M., Danica Bergin, Benoit Deflandre, Sagar Gupta, Joren J. C. Salazar, Richard Villagrana, Nudzejma Stulanovic, et al. "Role of Alternative Elicitor Transporters in the Onset of Plant Host Colonization by Streptomyces scabiei 87-22." Biology 12, no. 2 (February 1, 2023): 234. http://dx.doi.org/10.3390/biology12020234.

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Plant colonization by Streptomyces scabiei, the main cause of common scab disease on root and tuber crops, is triggered by cello-oligosaccharides, cellotriose being the most efficient elicitor. The import of cello-oligosaccharides via the ATP-binding cassette (ABC) transporter CebEFG-MsiK induces the production of thaxtomin phytotoxins, the central virulence determinants of this species, as well as many other metabolites that compose the ‘virulome’ of S. scabiei. Homology searches revealed paralogues of the CebEFG proteins, encoded by the cebEFG2 cluster, while another ABC-type transporter, PitEFG, is encoded on the pathogenicity island (PAI). We investigated the gene expression of these candidate alternative elicitor importers in S. scabiei 87-22 upon cello-oligosaccharide supply by transcriptomic analysis, which revealed that cebEFG2 expression is highly activated by both cellobiose and cellotriose, while pitEFG expression was barely induced. Accordingly, deletion of pitE had no impact on virulence and thaxtomin production under the conditions tested, while the deletion of cebEFG2 reduced virulence and thaxtomin production, though not as strong as the mutants of the main cello-oligosaccharide transporter cebEFG1. Our results thus suggest that both ceb clusters participate, at different levels, in importing the virulence elicitors, while PitEFG plays no role in this process under the conditions tested. Interestingly, under more complex culture conditions, the addition of cellobiose restored thaxtomin production when both ceb clusters were disabled, suggesting the existence of an additional mechanism that is involved in sensing or importing the elicitor of the onset of the pathogenic lifestyle of S. scabiei.

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7

BORASTON, Alisdair B., Mazyar GHAFFARI, R. Antony J. WARREN, and Douglas G. KILBURN. "Identification and glucan-binding properties of a new carbohydrate-binding module family." Biochemical Journal 361, no. 1 (December 17, 2001): 35–40. http://dx.doi.org/10.1042/bj3610035.

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The C-terminal 191-residue module of Cel5A from the alkalophilic Bacillus sp. 1139 comprises a carbohydrate-binding module (CBM) belonging to a previously unidentified family that we have classified as CBM family 28. This example, called CBM28, bound specifically to cello-oligosaccharides and mixed β-(1,3)(1,4)-glucans (barley β-glucan) with association constants of approximately (1–4)×104 M−1. Its binding to barley β-glucan was remarkably insensitive to pH between 7.0 and 10.9, in keeping with its alkalophilic source. CBM28 bound to cellulose having a significant non-crystalline content with an association constant similar to that for its binding to soluble glucans. CBM17 (CBM family 17) and CBM28 modules naturally occur as tandems. The CBM17/CBM28 tandem from Cel5A bound with apparent co-operativity to barley β-glucan. The association of CBM28 with cello-oligosaccharides was driven enthalpically and marked by the different thermodynamic contribution of three putative binding subsites that accommodate a cellohexaose molecule.

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8

Peri, Suma, Lakshmi Muthukumar, M. Nazmul Karim, and Rajesh Khare. "Dynamics of cello-oligosaccharides on a cellulose crystal surface." Cellulose 19, no. 6 (September 27, 2012): 1791–806. http://dx.doi.org/10.1007/s10570-012-9771-8.

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9

BORASTON, Alisdair B. "The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven." Biochemical Journal 385, no. 2 (January 7, 2005): 479–84. http://dx.doi.org/10.1042/bj20041473.

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Natural cellulose exists as a composite of cellulose forms, which can be broadly characterized as crystalline or non-crystalline. The recognition of both of these forms of cellulose by the CBMs (carbohydrate-binding modules) of microbial glycoside hydrolases is important for the efficient natural and biotechnological conversion of cellulosic biomass. The category of CBM that binds insoluble non-crystalline cellulose does so with an affinity approx. 10–20-fold greater than their affinity for cello-oligosaccharides and/or soluble polysaccharides. This phenomenon has been assumed to originate from the effects of changes in configurational entropy upon binding. The loss of configurational entropy is thought to be less profound upon binding to conformationally restrained insoluble non-crystalline cellulose, resulting in larger free energies of binding. However, using isothermal titration calorimetry, it is shown that this is not the case for the high-affinity interactions of CcCBM17 (the family 17 CBM from EngF of Clostridium cellulovorans) and BspCBM28 (the family 28 CBM from Cel5A of Bacillus species 1139) with regenerated cellulose, an insoluble preparation of primarily non-crystalline cellulose. The enhanced free energy of binding of non-crystalline cellulose relative to cello-oligosaccharides is by virtue of improved enthalpy, not entropy.

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10

Chen, Pengru, Abhijit Shrotri, and Atsushi Fukuoka. "Synthesis of cello-oligosaccharides by depolymerization of cellulose: A review." Applied Catalysis A: General 621 (July 2021): 118177. http://dx.doi.org/10.1016/j.apcata.2021.118177.

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11

Chen, Pengru, Abhijit Shrotri, and Atsushi Fukuoka. "Soluble Cello‐Oligosaccharides Produced by Carbon‐Catalyzed Hydrolysis of Cellulose." ChemSusChem 12, no. 12 (May 28, 2019): 2576–80. http://dx.doi.org/10.1002/cssc.201900800.

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12

BOLAM, David N., Antonio CIRUELA, Simon McQUEEN-MASON, Peter SIMPSON, Michael P. WILLIAMSON, Jane E. RIXON, Alisdair BORASTON, Geoffrey P. HAZLEWOOD, and Harry J. GILBERT. "Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity." Biochemical Journal 331, no. 3 (May 1, 1998): 775–81. http://dx.doi.org/10.1042/bj3310775.

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To investigate the mode of action of cellulose-binding domains (CBDs), the Type II CBD from Pseudomonas fluorescenssubsp. cellulosaxylanase A (XYLACBD) and cellulase E (CELECBD) were expressed as individual entities or fused to the catalytic domain of a Clostridium thermocellumendoglucanase (EGE). The two CBDs exhibited similar Ka values for bacterial microcrystalline cellulose (CELECBD, 1.62×106 M-1; XYLACBD, 1.83×106 M-1) and acid-swollen cellulose (CELECBD, 1.66×106 M-1; XYLACBD, 1.73×106 M-1). NMR spectra of XYLACBD titrated with cello-oligosaccharides showed that the environment of three tryptophan residues was affected when the CBD bound cellohexaose, cellopentaose or cellotetraose. The Ka values of the XYLACBD for C6, C5 and C4 cello-oligosaccharides were estimated to be 3.3×102, 1.4×102 and 4.0×101 M-1 respectively, suggesting that the CBD can accommodate at least six glucose molecules and has a much higher affinity for insoluble cellulose than soluble oligosaccharides. Fusion of either the CELECBD or XYLACBD to the catalytic domain of EGE potentiated the activity of the enzyme against insoluble forms of cellulose but not against carboxymethylcellulose. The increase in cellulase activity was not observed when the CBDs were incubated with the catalytic domain of either EGE or XYLA, with insoluble cellulose and a cellulose/hemicellulose complex respectively as the substrates. PseudomonasCBDs did not induce the extension of isolated plant cell walls nor weaken cellulose paper strips in the same way as a class of plant cell wall proteins called expansins. The XYLACBD and CELECBD did not release small particles from the surface of cotton. The significance of these results in relation to the mode of action of Type II CBDs is discussed.

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13

Ito, Fuyu, Yoshihiko Amano, Masahiro Shiroishi, Kouichi Nozaki, Inder M. Saxena, Malcolm R. Brown Jr., and Takahisa Kanda. "Accumulation of Cello-oligosaccharides during Bacterial Cellulose Production by Acetobacter xylinum." Journal of Applied Glycoscience 52, no. 1 (2005): 27–30. http://dx.doi.org/10.5458/jag.52.27.

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14

Wang, Chi-Huei, Tzong-Hsiung Hseu, and Chen-Ming Huang. "Induction of cellulase by cello-oligosaccharides in Trichoderma koningii G-39." Journal of Biotechnology 9, no. 1 (December 1988): 47–59. http://dx.doi.org/10.1016/0168-1656(88)90014-4.

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15

Liang, Xianxiang, Takashi Yoshida, and Toshiyuki Uryu. "Direct saccharification and ethanol fermentation of cello-oligosaccharides with recombinant yeast." Carbohydrate Polymers 91, no. 1 (January 2013): 157–61. http://dx.doi.org/10.1016/j.carbpol.2012.07.056.

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16

Liang, Yazhe, Wangli Ji, Xianhua Sun, Zhenzhen Hao, Xiaolu Wang, Yuan Wang, Wei Zhang, et al. "Production of cello-oligosaccharides from corncob residue by degradation-synthesis reactions." Applied Microbiology and Biotechnology 108, no. 1 (January 3, 2024): 1–11. http://dx.doi.org/10.1007/s00253-023-12832-6.

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17

Claeyssens, M., H. van Tilbeurgh, J. P. Kamerling, J. Berg, M. Vrsanska, and P. Biely. "Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I." Biochemical Journal 270, no. 1 (August 15, 1990): 251–56. http://dx.doi.org/10.1042/bj2700251.

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Endoglucanase I from the filamentous fungus Trichoderma reesei catalyses hydrolysis and glycosyl-transfer reactions of cello-oligosaccharides. Initial bond-cleaving frequencies determined with 1-3H-labelled cello-oligosaccharides proved to be substrate-concentration-dependent. Using chromophoric glycosides and analysing the reaction products by h.p.l.c., kinetic data are obtained and, as typical for an endo-type depolymerase, apparent hydrolytic parameters (kcat., kcat./Km) increase steadily as a function of the number of glucose residues. At high substrate concentrations, and for both free cellodextrins and their aromatic glycosides, complex patterns (transfer reactions) are, however, evident. In contrast with the corresponding lactosides and 1-thiocellobiosides, and in conflict with the expected specificity, aromatic 1-O-beta-cellobiosides are apparently hydrolysed at both scissile bonds, yielding the glucoside as one of the main reaction products. Its formation rate is clearly non-hyperbolically related to the substrate concentration and, since the rate of D-glucose formation is substantially lower, strong indications for dismutation reactions (self-transfer) are again obtained. Evidence for transfer reactions catalysed by endoglucanase I further results from experiments using different acceptor and donor substrates. A main transfer product accumulating in a digest containing a chromophoric 1-thioxyloside was isolated and its structure elucidated by proton n.m.r. spectrometry (500 MHz). The beta 1-4 configuration of the newly formed bond was proved.

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18

Kendrick, Emanuele G., Rakesh Bhatia, Fernando C. Barbosa, Rosana Goldbeck, Joe A. Gallagher, and David J. Leak. "Enzymatic generation of short chain cello-oligosaccharides from Miscanthus using different pretreatments." Bioresource Technology 358 (August 2022): 127399. http://dx.doi.org/10.1016/j.biortech.2022.127399.

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19

Lorences, Ester P., Gordon J. McDougall, and Stephen C. Fry. "Xylogliicae- and cello-oligosaccharides: Antagonists of the growth-promoting effect of H+." Physiologia Plantarum 80, no. 1 (September 1990): 109–13. http://dx.doi.org/10.1111/j.1399-3054.1990.tb04382.x.

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20

Lorences, Ester P., Gordon J. McDougall, and Stephen C. Fry. "Xyloglucan- and cello-oligosaccharides: Antagonists of the growth-promoting effect of H+." Physiologia Plantarum 80, no. 1 (September 1990): 109–13. http://dx.doi.org/10.1034/j.1399-3054.1990.800117.x.

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21

Cao, Ruyin, Yongdong Jin, and Dingguo Xu. "Recognition of Cello-Oligosaccharides by CBM17 from Clostridium cellulovorans: Molecular Dynamics Simulation." Journal of Physical Chemistry B 116, no. 21 (May 18, 2012): 6087–96. http://dx.doi.org/10.1021/jp3010647.

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22

Hommalai, Greanggrai, Stephen G. Withers, Watchalee Chuenchor, James R. Ketudat Cairns, and Jisnuson Svasti. "Enzymatic synthesis of cello-oligosaccharides by rice BGlu1 β-glucosidase glycosynthase mutants." Glycobiology 17, no. 7 (April 3, 2007): 744–53. http://dx.doi.org/10.1093/glycob/cwm039.

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23

Tominaga, Rumi, Masahiro Samejima, Fukumi Sakai, and Takahisa Hayashi. "Occurrence of Cello-Oligosaccharides in the Apoplast of Auxin-Treated Pea Stems." Plant Physiology 119, no. 1 (January 1, 1999): 249–54. http://dx.doi.org/10.1104/pp.119.1.249.

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24

Vrs̆anská, Mária, and Peter Biely. "The cellobiohydrolase I from Trichoderma reesei QM 9414: action on cello-oligosaccharides." Carbohydrate Research 227 (April 1992): 19–27. http://dx.doi.org/10.1016/0008-6215(92)85058-8.

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25

Isaksen, Trine, Bjørge Westereng, Finn L. Aachmann, Jane W. Agger, Daniel Kracher, Roman Kittl, Roland Ludwig, Dietmar Haltrich, Vincent G. H. Eijsink, and Svein J. Horn. "A C4-oxidizing Lytic Polysaccharide Monooxygenase Cleaving Both Cellulose and Cello-oligosaccharides." Journal of Biological Chemistry 289, no. 5 (December 9, 2013): 2632–42. http://dx.doi.org/10.1074/jbc.m113.530196.

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26

Claeyssens, M., H. Van Tilbeurgh, P. Tomme, T. M. Wood, and S. I. McRae. "Fungal cellulase systems. Comparison of the specificities of the cellobiohydrolases isolated from Penicillium pinophilum and Trichoderma reesei." Biochemical Journal 261, no. 3 (August 1, 1989): 819–25. http://dx.doi.org/10.1042/bj2610819.

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Reaction patterns for the hydrolysis of chromophoric glycosides from cello-oligosaccharides and lactose by the cellobiohydrolases (CBH I and CBH II) purified from Trichoderma reesei and Penicillium pinophilum were determined. They coincide with those found for the parent unsubstituted sugars. CBH I enzyme from both organisms attacks these substrates in a random manner. Turnover numbers are, however, low and do not increase appreciably as a function of the degree of polymerization of the substrates. The active-site topology of the CBH I from T. reesei was further probed by equilibrium binding experiments with cellobiose, cellotriose, lactose and some of their derivatives. These point to a single interaction site (ABC), spatially restricted as deduced from the apparent independency of the thermodynamic parameters. It appears that the putative subsite A can accommodate a galactopyranosyl or glucopyranosyl group, and subsite B a glucopyranosyl group, whereas in subsite C either a glucopyranosyl or a chromophoric group can be bound, scission occurring between subsites B and C. The apparent kinetic parameters (turnover numbers) for the hydrolysis of cello-oligosaccharides (and their derivatives) by the CBH II type enzyme increase as a function of chain length, indicative of an extended binding site (A-F). Its architecture allows for specific binding of beta-(1-4)-glucopyranosyl groups in subsites A, B and C. Binding of a chromophore in subsite C produces a non-hydrolysable complex. The thermodynamic interaction parameters of some ligands common to both type of enzyme were compared: these substantiate the conclusions reached above.

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27

Deflandre, Benoit, and Sébastien Rigali. "Old Enzyme, New Role: The β-Glucosidase BglC of Streptomyces scabiei Interferes with the Plant Defense Mechanism by Hydrolyzing Scopolin." Biophysica 2, no. 1 (December 22, 2021): 1–7. http://dx.doi.org/10.3390/biophysica2010001.

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The beta-glucosidase BglC fulfills multiple functions in both primary metabolism and induction of pathogenicity of Streptomyces scabiei, the causative agent of common scab in root and tuber crops. Indeed, this enzyme hydrolyzes cellobiose and cellotriose to feed glycolysis with glucose directly and modifies the intracellular concentration of these cello-oligosaccharides, which are the virulence elicitors. The inactivation of bglC led to unexpected phenotypes such as the constitutive overproduction of thaxtomin A, the main virulence determinant of S. scabiei. In this work, we reveal a new target substrate of BglC, the phytoalexin scopolin. Removal of the glucose moiety of scopolin generates scopoletin, a potent inhibitor of thaxtomin A production. The hydrolysis of scopolin by BglC displayed substrate inhibition kinetics, which contrasts with the typical Michaelis–Menten saturation curve previously observed for the degradation of its natural substrate cellobiose. Our work, therefore, reveals that BglC targets both cello-oligosaccharide elicitors emanating from the hosts of S. scabiei, and the scopolin phytoalexin generated by the host defense mechanisms, thereby occupying a key position to fine-tune the production of the main virulence determinant thaxtomin A.

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28

Johnson, Evan G., Madhumita V. Joshi, Donna M. Gibson, and Rosemary Loria. "Cello-oligosaccharides released from host plants induce pathogenicity in scab-causing Streptomyces species." Physiological and Molecular Plant Pathology 71, no. 1-3 (July 2007): 18–25. http://dx.doi.org/10.1016/j.pmpp.2007.09.003.

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29

Westereng, Bjørge, Jane Wittrup Agger, Svein J. Horn, Gustav Vaaje-Kolstad, Finn L. Aachmann, Yngve H. Stenstrøm, and Vincent G. H. Eijsink. "Efficient separation of oxidized cello-oligosaccharides generated by cellulose degrading lytic polysaccharide monooxygenases." Journal of Chromatography A 1271, no. 1 (January 2013): 144–52. http://dx.doi.org/10.1016/j.chroma.2012.11.048.

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30

Kuba, Yoshinori, Yutaka Kashiwagi, Gentaro Okada, and Takashi Sasaki. "Production of cello-oligosaccharides by enzymatic hydrolysis in the presence of activated carbon." Enzyme and Microbial Technology 12, no. 1 (January 1990): 72–75. http://dx.doi.org/10.1016/0141-0229(90)90183-q.

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31

Qi, Meng, Hyun-Sik Jun, and Cecil W. Forsberg. "Cel9D, an Atypical 1,4-β-d-Glucan Glucohydrolase from Fibrobacter succinogenes: Characteristics, Catalytic Residues, and Synergistic Interactions with Other Cellulases." Journal of Bacteriology 190, no. 6 (January 18, 2008): 1976–84. http://dx.doi.org/10.1128/jb.01667-07.

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ABSTRACT The increasing demands of renewable energy have led to the critical emphasis on novel enzymes to enhance cellulose biodegradation for biomass conversion. To identify new cellulases in the ruminal bacterium Fibrobacter succinogenes, a cell extract of cellulose-grown cells was separated by ion-exchange chromatography and cellulases were located by zymogram analysis and identified by peptide mass fingerprinting. An atypical family 9 glycoside hydrolase (GH9), Cel9D, with less than 20% identity to typical GH9 cellulases, was identified. Purified recombinant Cel9D enhanced the production of reducing sugar from acid swollen cellulose (ASC) and Avicel by 1.5- to 4-fold when mixed separately with each of four other glucanases, although it had low activity on these substrates. Cel9D degraded ASC and cellodextrins with a degree of polymerization higher than 2 to glucose with no apparent endoglucanase activity, and its activity was restricted to β-1→4-linked glucose residues. It catalyzed the hydrolysis of cellulose by an inverting mode of reaction, releasing glucose from the nonreducing end. Unlike many GH9 cellulases, calcium ions were not required for its function. Cel9D had increased k cat /K m values for cello-oligosaccharides with higher degrees of polymerization. The k cat /K m value for cellohexaose was 2,300 times higher than that on cellobiose. This result indicates that Cel9D is a 1,4-β-d-glucan glucohydrolase (EC 3.2.1.74) in the GH9 family. Site-directed mutagenesis of Cel9D identified Asp166 and Glu612 as the candidate catalytic residues, while Ser168, which is not present in typical GH9 cellulases, has a crucial structural role. This enzyme has an important role in crystalline cellulose digestion by releasing glucose from accessible cello-oligosaccharides.

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32

PARRY, Neil J., David E. BEEVER, Emyr OWEN, Isabel VANDENBERGHE, Jozef VAN BEEUMEN, and Mahalingeshwara K. BHAT. "Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus." Biochemical Journal 353, no. 1 (December 18, 2000): 117–27. http://dx.doi.org/10.1042/bj3530117.

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An extracellular β-glucosidase from Thermoascus aurantiacus was purified to homogeneity by DEAE-Sepharose, Ultrogel AcA 44 and Mono-P column chromatography. The enzyme was a homotrimer, with a monomer molecular mass of 120kDa; only the trimer was optimally active at 80°C and at pH 4.5. At 90°C, the enzyme showed 70% of its optimal activity. It was stable at pH 5.2 and at temperatures up to 70°C for 48h, but stability decreased above 70°C and at pH values above and below 5.0. The enzyme hydrolysed aryl and alkyl β-d-glucosides and cello-oligosaccharides, and was specific for substrates with a β-glycosidic linkage. The hydroxy groups at positions 2, 4 and 6 of a glucose residue at the non-reducing end of a disaccharide appeared to be essential for catalysis. The enzyme had the lowest Km towards p-nitrophenyl β-d-glucoside (0.1137mM) and the highest kcat towards cellobiose and β,β-trehalose (17052min-1). It released one glucose unit at a time from the non-reducing end of cello-oligosaccharides, and the rate of hydrolysis decreased with an increase in chain length. Glucose and d-δ-gluconolactone inhibited the β-glucosidase competitively, with Ki values of 0.29mM and 8.3nM respectively, while methanol, ethanol and propan-2-ol activated the enzyme. The enzyme catalysed the synthesis of methyl, ethyl and propyl β-d-glucosides in the presence of methanol, ethanol and propan-2-ol respectively with either glucose or cellobiose, although cellobiose was preferred. An acidic pH favoured hydrolysis and transglycosylation, but high concentrations of alcohols favoured the latter reaction. The stereochemistry of cellobiose hydrolysis revealed that β-glucosidase from T. aurantiacus is a retaining glycosidase, while N-terminal amino acid sequence alignment indicated that it is a member of glycoside hydrolase family 3.

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33

Ávila, Patrícia F., and Rosana Goldbeck. "Fractionating process of lignocellulosic biomass for the enzymatic production of short chain cello-oligosaccharides." Industrial Crops and Products 178 (April 2022): 114671. http://dx.doi.org/10.1016/j.indcrop.2022.114671.

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34

Im, Hee Jin, Choon Young Kim, and Kyung Young Yoon. "Production and Characteristics of Cello- and Xylo-oligosaccharides by Enzymatic Hydrolysis of Buckwheat Hulls." Korean Journal of Food Science and Technology 48, no. 3 (June 30, 2016): 201–7. http://dx.doi.org/10.9721/kjfst.2016.48.3.201.

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35

Zhong, Chao, Božidar Duić, Juan M. Bolivar, and Bernd Nidetzky. "Three‐Enzyme Phosphorylase Cascade Immobilized on Solid Support for Biocatalytic Synthesis of Cello−oligosaccharides." ChemCatChem 12, no. 5 (January 22, 2020): 1350–58. http://dx.doi.org/10.1002/cctc.201901964.

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Li, Qiuyue, Jiawen Chang, Peiwen Lv, Junxia Li, Yuxia Duan, Dandan Tian, Fei Ge, et al. "Physiological Functions of the Cello-Oligosaccharides Binding CebE in the Pathogenic Streptomyces sp. AMCC400023." Microorganisms 12, no. 3 (February 29, 2024): 499. http://dx.doi.org/10.3390/microorganisms12030499.

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Potato common scab, an economically important disease worldwide, is caused by pathogenic Streptomyces strains mainly through the effects of thaxtomin. The cello-oligosaccharides binding protein CebE is proposed as a gateway to the pathogenic development of Streptomyces scabiei. In this study, two functional CebE encoding genes, GEO5601 and GEO7671, were identified in pathogenic Streptomyces sp. AMCC400023. With a higher binding affinity towards signal molecules, the deletion of GEO5601 severely impaired thaxtomin-producing capacity and reduced the strain’s pathogenicity. Transcriptional analysis confirmed that CebE5601 is also responsible for the import and provision of carbon sources for cell growth. With lower binding affinity, the pathogenicity island (PAI)-localized CebE7671 may assume a new function of mediating the biological process of sporulation, given the significantly impaired formation of ΔGEO7671 spores. The mechanisms of action of CebE proteins unraveled in Streptomyces sp. AMCC400023 will help pave the way for more effective prevention of the potato common scab disease.

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Karnaouri, Anthi, Leonidas Matsakas, Saskja Bühler, Madhu Nair Muraleedharan, Paul Christakopoulos, and Ulrika Rova. "Tailoring Celluclast® Cocktail’s Performance towards the Production of Prebiotic Cello-Oligosaccharides from Waste Forest Biomass." Catalysts 9, no. 11 (October 28, 2019): 897. http://dx.doi.org/10.3390/catal9110897.

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The main objective of this study focused on the sustainable production of cellobiose and other cellulose-derived oligosaccharides from non-edible sources, more specifically, from forest residues. For this purpose, a fine-tuning of the performance of the commercially available enzyme mixture Celluclast® was conducted towards the optimization of cellobiose production. By enzyme reaction engineering (pH, multi-stage hydrolysis with buffer exchange, addition of β-glucosidase inhibitor), a cellobiose-rich product with a high cellobiose to glucose ratio (37.4) was achieved by utilizing organosolv-pretreated birch biomass. In this way, controlled enzymatic hydrolysis combined with efficient downstream processing, including product recovery and purification through ultrafiltration and nanofiltration, can potentially support the sustainable production of food-grade oligosaccharides from forest biomass. The potential of the hydrolysis product to support the growth of two Lactobacilli probiotic strains as a sole carbon source was also demonstrated.

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Karim, Nurul, and Shun-ichi Kidokoro. "Precise and continuous observation of cellulase-catalyzed hydrolysis of cello-oligosaccharides using isothermal titration calorimetry." Thermochimica Acta 412, no. 1-2 (March 2004): 91–96. http://dx.doi.org/10.1016/j.tca.2003.09.001.

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Barbosa, Fernando César, Manoela Martins, Lívia Beatriz Brenelli, Felipe Augusto Ferrari, Marcus Bruno Soares Forte, Sarita Cândida Rabelo, Telma Teixeira Franco, and Rosana Goldbeck. "Screening of potential endoglucanases, hydrolysis conditions and different sugarcane straws pretreatments for cello-oligosaccharides production." Bioresource Technology 316 (November 2020): 123918. http://dx.doi.org/10.1016/j.biortech.2020.123918.

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Mallek-Fakhfakh, Hanen, and Hafedh Belghith. "Physicochemical properties of thermotolerant extracellular β-glucosidase from Talaromyces thermophilus and enzymatic synthesis of cello-oligosaccharides." Carbohydrate Research 419 (January 2016): 41–50. http://dx.doi.org/10.1016/j.carres.2015.10.014.

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Bey, Mathieu, Simeng Zhou, Laetitia Poidevin, Bernard Henrissat, Pedro M. Coutinho, Jean-Guy Berrin, and Jean-Claude Sigoillot. "Cello-Oligosaccharide Oxidation Reveals Differences between Two Lytic Polysaccharide Monooxygenases (Family GH61) from Podospora anserina." Applied and Environmental Microbiology 79, no. 2 (November 2, 2012): 488–96. http://dx.doi.org/10.1128/aem.02942-12.

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ABSTRACTThe genome of the coprophilic ascomycetePodospora anserinaencodes 33 different genes encoding copper-dependent lytic polysaccharide monooxygenases (LPMOs) from glycoside hydrolase family 61 (GH61). In this study, two of these enzymes (P. anserinaGH61A [PaGH61A] andPaGH61B), which both harbored a family 1 carbohydrate binding module, were successfully produced inPichia pastoris. Synergistic cooperation betweenPaGH61A orPaGH61B with the cellobiose dehydrogenase (CDH) ofPycnoporus cinnabarinuson cellulose resulted in the formation of oxidized and nonoxidized cello-oligosaccharides. A striking difference betweenPaGH61A andPaGH61B was observed through the identification of the products, among which were doubly and triply oxidized cellodextrins, which were released only by the combination ofPaGH61B with CDH. The mass spectrometry fragmentation patterns of these oxidized products could be consistent with oxidation at the C-6 position with a geminal diol group. The different properties ofPaGH61A andPaGH61B and their effect on the interaction with CDH are discussed in regard to the proposedin vivofunction of the CDH/GH61 enzyme system in oxidative cellulose hydrolysis.

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CHIRICO, William J., and Ross D. BROWN. "beta-Glucosidase from Trichoderma reesei. Substrate-binding region and mode of action on [1-3H]cello-oligosaccharides." European Journal of Biochemistry 165, no. 2 (June 1987): 343–51. http://dx.doi.org/10.1111/j.1432-1033.1987.tb11447.x.

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Ikura, Mitsuhiko, and Kunio Hikichi. "Two-dimensional 1H-N.M.R. studies of cello-oligosaccharides: The utility of multiple-relay chemical-shift-correlated spectroscopy." Carbohydrate Research 163, no. 1 (June 1987): 1–8. http://dx.doi.org/10.1016/0008-6215(87)80159-3.

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Striegel, André M., and Marcus A. Boone. "Influence of glycosidic linkage on solution conformational entropy of oligosaccharides: Malto- vs. isomalto- and cello- vs. laminarioligosaccharides." Biopolymers 95, no. 4 (November 17, 2010): 228–33. http://dx.doi.org/10.1002/bip.21567.

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Liu, Xueqing, Kevin K. Y. Hu, and Victoria S. Haritos. "Enzymatic production of cello-oligosaccharides with potential human prebiotic activity and release of polyphenols from grape marc." Food Chemistry 435 (March 2024): 137562. http://dx.doi.org/10.1016/j.foodchem.2023.137562.

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Kosugi, Akihiko, Takamitsu Arai, and Roy H. Doi. "Degradation of cellulosome-produced cello-oligosaccharides by an extracellular non-cellulosomal β-glucan glucohydrolase, BglA, from Clostridium cellulovorans." Biochemical and Biophysical Research Communications 349, no. 1 (October 2006): 20–23. http://dx.doi.org/10.1016/j.bbrc.2006.07.038.

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Kamitakahara, Hiroshi, Fumiaki Nakatsubo, and Dieter Klemm. "New class of carbohydrate-based nonionic surfactants: diblock co-oligomers of tri-O-methylated and unmodified cello-oligosaccharides." Cellulose 14, no. 5 (June 13, 2007): 513–28. http://dx.doi.org/10.1007/s10570-007-9128-x.

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Kamitakahara, Hiroshi, and Fumiaki Nakatsubo. "ABA- and BAB-triblock cooligomers of tri-O-methylated and unmodified cello-oligosaccharides: syntheses and structure-solubility relationship." Cellulose 17, no. 1 (August 8, 2009): 173–86. http://dx.doi.org/10.1007/s10570-009-9348-3.

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Barbosa, Fernando Cesar, Emanuele Kendrick, Livia Beatriz Brenelli, Henrique Silvano Arruda, Glaucia Maria Pastore, Sarita Cândida Rabelo, André Damasio, Telma Teixeira Franco, David Leak, and Rosana Goldbeck. "Optimization of cello-oligosaccharides production by enzymatic hydrolysis of hydrothermally pretreated sugarcane straw using cellulolytic and oxidative enzymes." Biomass and Bioenergy 141 (October 2020): 105697. http://dx.doi.org/10.1016/j.biombioe.2020.105697.

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Sun, Peicheng, Matthias Frommhagen, Maloe Kleine Haar, Gijs van Erven, Edwin J. Bakx, Willem J. H. van Berkel, and Mirjam A. Kabel. "Mass spectrometric fragmentation patterns discriminate C1- and C4-oxidised cello-oligosaccharides from their non-oxidised and reduced forms." Carbohydrate Polymers 234 (April 2020): 115917. http://dx.doi.org/10.1016/j.carbpol.2020.115917.

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