492-62-6Relevant articles and documents
Two new triterpenoid glycosides from Curculigo orchioides
Zuo, Ai-Xue,Shen, Yong,Jiang, Zhi-Yong,Zhang, Xue-Mei,Zhou, Jun,Lue, Jun,Chen, Ji-Jun
, p. 407 - 412 (2012)
Two new cycloartane triterpenoid glycosides, named curculigosaponin N and curculigosaponin O, were isolated from rhizomes of Curculigo orchioides Gaertn. Their structures were elucidated on the basis of comprehensive spectroscopic analysis including IR, M
Microbial production of neryl-α-D-glucopyranoside from nerol by Agrobacterium sp. M-12 reflects glucosyl transfer activity
Takahashi, Kazuki,Terauchi, Issei,Ono, Marie,Satoh, Hiroshi,Ueda, Makoto
, p. 2205 - 2211 (2018)
Terpene alcohol is widely used in perfumes and is known to possess antibacterial activity. Moreover, in its glycosylated form, it can be applied as a nonionic surfactant in food, and in the pharmaceutical, chemical, cosmetic, and detergent industries. Presently, chemical production of terpene glucosides is hampered by high costs and low yields. Here, we investigated the microbial glucosylation of nerol (cis-3,7-dimethylocta-2,6-dien-1-ol), a component of volatile oils, by Agrobacterium sp. M-12 isolated from soil. A microbial reaction using washed cells of Agrobacterium sp. M-12, 1 g/L of nerol, and 100 g/L of maltose under optimal conditions yielded 1.8 g/L of neryl-α-D-glucopyranoside after 72 h. The molar yield of neryl-α-D-glucopyranoside was 87.6%. Additionally, we report the successful transglucosylation of other monoterpene alcohols, such as geraniol, (-)-β-citro-nellol, and (-)-linalool, by Agrobacterium sp. M-12. Thus, microbial glucosylation has potential widespread applicability for efficient, low-cost production of glycosylated terpene alcohols.
Aryl sulfonic acid catalyzed hydrolysis of cellulose in water
Amarasekara, Ananda S.,Wiredu, Bernard
, p. 259 - 262 (2012)
Catalytic activities of eight alkyl/aryl sulfonic acids in water were compared with sulfuric acid of the same acid strength (0.0321 mol H+ ion/L) for hydrolysis of Sigmacell cellulose (DP ～ 450) in the 140-190 °C temperature range by measuring total reducing sugar (TRS), and glucose produced. Cellulose samples hydrolyzed at 160 °C for 3 h, in aqueous p-toluenesulfonic acid, 2-naphthalenesulfonic acid, and 4-biphenylsulfonic acid mediums produced TRS yields of 28.0, 25.4, and 30.3% respectively, when compared to 21.7% TRS produced in aqueous sulfuric acid medium. The first order rate constants at 160 °C in different acid mediums correlated with octanol/water distribution coefficient log D of these acids, except in the case of highly hydrophobic 4-dodceylbenzenesulfonic acid. In the series of sulfonic acids studied, 4-biphenylsulfonic acid appears to be the best cellulose hydrolysis catalyst.
Immobilized cellulase on Fe3O4 nanoparticles as a magnetically recoverable biocatalyst for the decomposition of corncob
Zhang, Qikun,Kang, Junqing,Yang, Bing,Zhao, Leizhen,Hou, Zhaosheng,Tang, Bo
, p. 389 - 397 (2016)
A magnetically recoverable biocatalyst was successfully prepared through the immobilization of cellulase onto Fe3O4 nanoparticles. The magnetic nanoparticles were synthesized by a hydrothermal method in an aqueous system. The support (Fe3O4 nanoparticles) was modified with (3-aminopropyl)triethoxysilane, and glutaraldehyde was used as the cross-linker to immobilize the cellulose onto the modified support. Different factors that influence the activity of the immobilized enzyme were investigated. The experimental results indicated that the suitable immobilization temperature and pH are 40 °C and 6.0, respectively. The optimal glutaraldehyde concentration is ～2.0 wt%, and the appropriate immobilization time is 4 h. Under these optimal conditions, the activity of the immobilized enzyme could be maintained at 99.1% of that of the free enzyme. Moreover, after 15 cyclic runs, the activity of the immobilized enzyme was maintained at ～91.1%. The prepared biocatalyst was used to decompose corncobs, and the maximum decomposition rate achieved was 61.94%.
Flavonoid glucuronides and a chromone from the aquatic macrophyte Stratiotes aloides
Conrad, Juergen,Foerster-Fromme, Bernhard,Constantin, Mihaela-Anca,Ondrus, Vladimir,Mika, Sabine,Mert-Balci, Fadime,Klaiber, Iris,Pfannstiel, Jens,Moeller, Wolfgang,Roesner, Harald,Foerster-Fromme, Karin,Beifuss, Uwe
, p. 835 - 840 (2009)
The first phytochemical analysis of the aquatic macrophyte Stratiotes aloides afforded two new flavonoid glucuronides, luteolin 7-O-β-D- glucopyranosiduronic acid-(12)-β-D-glucopyranoside (1) and chrysoeriol 7-O-β-D-glucopyranosiduronic acid-(12)-β-D- glu
Hydrolysis of α- and β-D-glucosyl fluoride by individual glucosidases: new evidence for separately controlled "plastic" and "conserved" phases in glycosylase catalysis
Matsui, Hirokazu,Tanaka, Yoshimasa,Brewer, Curtis F.,Blanchard, John S.,Hehre, Edward J.
, p. 45 - 56 (1993)
α-Glucosidases from sugar beet seed and ungerminated rice catalyzed the hydrolysis of β-D-glucopyranosyl fluoride to form α-D-glucose.The reactions were slow, with V/K = 11-15 x 10-3 or ca. 1-2percent of that for hydrolysis of p-nitrophenyl α-D-glucopyranoside, but were not due to any impurity in the substrate of to contaminating β-glucosidase or glucomylase.Furthermore, almond β-glucosidase promoted hydrolysis of α-D-glucosyl fluoride to form β-D-glucose at an exceedingly low rate, V/K = 4 x 10-4.This weak reaction did not stem from any impurity in the substrate or to contamination with α-glucosidase or glucomylase, but it was partly (ca. 20percent) attributable to a trace of accompanying trehalase.That all three glucosidases acted upon both α- and β-D-glucosyl fluoride, albeit at low efficiency with the disfavored anomer, reflects the previously demonstrated ability of each enzyme's catalytic groups to respond flexibly to substrates of different types.That the disfavored D-glucosyl fluoride in each case was converted into a product of the same configuration as from enitols or favored D-glucosyl substrates provides additional evidence for the two-step nature of the chemical mechanisms of glucosidases, in which the stereochemistry of water attack on the enzyme-stabilized oxocarbonium ion is strictly maintained, regardless of the initial anomeric configuration of the substrate.
Structural elements responsible for the glucosidic linkage-selectivity of a glycoside hydrolase family 13 exo-glucosidase
Saburi, Wataru,Rachi-Otsuka, Hiroaki,Hondoh, Hironori,Okuyama, Masayuki,Mori, Haruhide,Kimura, Atsuo
, p. 865 - 869 (2015)
Abstract Glycoside hydrolase family 13 contains exo-glucosidases specific for α-(1 → 4)- and α-(1 → 6)-linkages including α-glucosidase, oligo-1,6-glucosidase, and dextran glucosidase. The α-(1 → 6)-linkage selectivity of Streptococcus mutans dextran glucosidase was altered to α-(1 → 4)-linkage selectivity through site-directed mutations at Val195, Lys275, and Glu371. V195A showed 1300-fold higher kcat/Km for maltose than wild-type, but its kcat/Km for isomaltose remained 2-fold higher than for maltose. K275A and E371A combined with V195A mutation only decreased isomaltase activity. V195A/K275A, V195A/E371A, and V195A/K275A/E371A showed 27-, 26-, and 73-fold higher kcat/Km for maltose than for isomaltose, respectively. Consequently, the three residues are structural elements for recognition of the α-(1 → 6)-glucosidic linkage.
Gluconic acid from biomass fast pyrolysis oils: Specialty chemicals from the thermochemical conversion of biomass
Santhanaraj, Daniel,Rover, Marjorie R.,Resasco, Daniel E.,Brown, Robert C.,Crossley, Steven
, p. 3132 - 3137 (2014)
Fast pyrolysis of biomass to produce a bio-oil followed by catalytic upgrading is a widely studied approach for the potential production of fuels from biomass. Because of the complexity of the bio-oil, most upgrading strategies focus on removing oxygen from the entire mixture to produce fuels. Here we report a novel method for the production of the specialty chemical, gluconic acid, from the pyrolysis of biomass. Through a combination of sequential condensation of pyrolysis vapors and water extraction, a solution rich in levoglucosan is obtained that accounts for over 30% of the carbon in the biooil produced from red oak. A simple filtration step yields a stream of high-purity levoglucosan. This stream of levoglucosan is then hydrolyzed and partially oxidized to yield gluconic acid with high purity and selectivity. This combination of costeffective pyrolysis coupled with simple separation and upgrading could enable a variety of new product markets for chemicals from biomass.
Acremonoside, a phenolic glucoside from the sea fan-derived fungus Acremonium polychromum PSU-F125
Khamthong, Nanthaphong,Rukachaisirikul, Vatcharin,Pakawatchai, Chaveng,Saithong, Saowanit,Phongpaichit, Souwalak,Preedanon, Sita,Sakayaroj, Jariya
, p. 50 - 54 (2014)
A new phenolic glucoside, acremonoside (1), along with two known compounds, F-11334 A2and 2,2-dimethyl-2H-chromen-6-ol, were isolated from the sea fan-derived fungus Acremonium polychromum PSU-F125. The structure of 1 was elucidated by spectroscopic techniques, acid hydrolysis and X-ray crystallographic analysis. The isolated compounds were tested for antibacterial, antimalarial, antimycobacterial and cytotoxic activities.
Catalytic properties and amino acid sequence of endo-1→3-β-D- glucanase from the marine mollusk Tapes literata
Zakharenko, A. M.,Kusaykin, M. I.,Kovalchuk, S. N.,Sova, V. V.,Silchenko, A. S.,Anastyuk, S. D.,Rasskazov, V. A.,Zvyagintseva, T. N.,Belik, A. A.,Ly, Bui Minh
, p. 878 - 888,11 (2012)
A specific 1→3-β-D-glucanase with molecular mass 37 kDa was isolated in homogeneous state from crystalline style of the commercial marine mollusk Tapes literata. It exhibits maximal activity within the pH range from 4.5 to 7.5 at 45°C. The 1→3-β-D-glucanase catalyzes hydrolysis of β-1?3 bonds in glucans as an endoenzyme with retention of bond configuration, and it has transglycosylating activity. The Km for hydrolysis of laminaran is 0.25 mg/ml. The enzyme is clas- sified as a glucan endo-(1→3)-β-D-glucosidase (EC 3.2.1.39). The cDNA encoding this 1→3-β-D-glucanase from T. lit- erata was sequenced, and the amino acid sequence of the enzyme was determined. The endo-1→3-β-D-glucanase from T. literata was assigned to the 16th structural family (GHF 16) of O-glycoside hydrolases.
