scholarly journals Synthesis of novel oligomeric anionic alkyl glycosides using laccase/TEMPO oxidation and cyclodextrin glucanotransferase (CGTase)‐catalysed transglycosylation

2021 ◽  
Author(s):  
Ngoc T. N. Ngo ◽  
Javier A. Linares‐Pastén ◽  
Carl Grey ◽  
Patrick Adlercreutz
Keyword(s):  
Cyclodextrin Glucanotransferase ◽  
Tempo Oxidation ◽  
Alkyl Glycosides

scholarly journals Efficient laccase/TEMPO oxidation of alkyl glycosides: Effects of carbohydrate group and alkyl chain length

2020 ◽  
Vol 8 ◽  
pp. 100026
Author(s):  
Ngoc T.N. Ngo ◽  
Carl Grey ◽  
Patrick Adlercreutz
Keyword(s):  
Chain Length ◽  
Alkyl Chain ◽  
Alkyl Chain Length ◽  
Tempo Oxidation ◽  
Alkyl Glycosides

scholarly journals One-Pot Bi-Enzymatic Cascade Synthesis of Novel Ganoderma Triterpenoid Saponins

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 580
Author(s):  
Te-Sheng Chang ◽  
Chien-Min Chiang ◽  
Tzi-Yuan Wang ◽  
Yu-Li Tsai ◽  
Yu-Wei Wu ◽  
...  
Keyword(s):  
High Performance ◽  
Aqueous Solubility ◽  
Major Product ◽  
Cyclodextrin Glucanotransferase ◽  
Bioactive Constituents ◽  
Ganoderic Acid ◽  
One Pot ◽  
Triterpenoid Saponins ◽  
Medicinal Fungus ◽  
Triterpenoid Glycosides

Ganoderma lucidum is a medicinal fungus whose numerous triterpenoids are its main bioactive constituents. Although hundreds of Ganoderma triterpenoids have been identified, Ganoderma triterpenoid glycosides, also named triterpenoid saponins, have been rarely found. Ganoderic acid A (GAA), a major Ganoderma triterpenoid, was synthetically cascaded to form GAA-15-O-β-glucopyranoside (GAA-15-G) by glycosyltransferase (BtGT_16345) from Bacillus thuringiensis GA A07 and subsequently biotransformed into a series of GAA glucosides by cyclodextrin glucanotransferase (Toruzyme® 3.0 L) from Thermoanaerobacter sp. The optimal reaction conditions for the second-step biotransformation of GAA-15-G were found to be 20% of maltose; pH 5; 60 °C. A series of GAA glucosides (GAA-G2, GAA-G3, and GAA-G4) could be purified with preparative high-performance liquid chromatography (HPLC) and identified by mass and nucleic magnetic resonance (NMR) spectral analysis. The major product, GAA-15-O-[α-glucopyranosyl-(1→4)-β-glucopyranoside] (GAA-G2), showed over 4554-fold higher aqueous solubility than GAA. The present study demonstrated that multiple Ganoderma triterpenoid saponins could be produced by sequential actions of BtGT_16345 and Toruzyme®, and the synthetic strategy that we proposed might be applied to many other Ganoderma triterpenoids to produce numerous novel Ganoderma triterpenoid saponins in the future.

scholarly journals A molecular scale analysis of TEMPO-oxidation of native cellulose molecules

Heliyon ◽  
2020 ◽  
Vol 6 (12) ◽  
pp. e05776
Author(s):  
Milad Asgarpour Khansary ◽  
Peyman Pouresmaeel-Selakjani ◽  
Mohammad Ali Aroon ◽  
Ahmad Hallajisani ◽  
Jennifer Cookman ◽  
...  
Keyword(s):  
Scale Analysis ◽  
Tempo Oxidation ◽  
Native Cellulose ◽  
Molecular Scale

scholarly journals Water-Soluble Constituents of Fennel. I. Alkyl Glycosides.

1998 ◽  
Vol 46 (10) ◽  
pp. 1643-1646 ◽  
Author(s):  
Junichi KITAJIMA ◽  
Toru ISHIKAWA ◽  
Yasuko TANAKA
Keyword(s):  
Water Soluble ◽  
Alkyl Glycosides

scholarly journals Enzymatic Synthesis and Anti-Allergic Activities of Curcumin Oligosaccharides

2010 ◽  
Vol 3 ◽  
pp. BCI.S2768 ◽  
Author(s):  
Kei Shimoda ◽  
Hiroki Hamada
Keyword(s):  
Mast Cells ◽  
Histamine Release ◽  
Enzymatic Synthesis ◽  
Antibody Formation ◽  
Cyclodextrin Glucanotransferase ◽  
Enzymatic Method ◽  
Inhibitory Effects ◽  
Peritoneal Mast Cells ◽  
Rat Peritoneal Mast Cells ◽  
Suppressive Action

Curcumin 4‘- O-glucooligosaccharides were synthesized by a two step-enzymatic method using almond β-glucosidase and cyclodextrin glucanotransferase (CGTase). Curcumin was glucosylated to curcumin 4‘- O-β-D-glucopyranoside by almond β-glucosidase in 19% yield. Curcumin 4‘- O-β-D-glucopyranoside was converted into curcumin 4‘- O-β-glucooligosaccharides, i.e. 4‘- O-β-maltoside (51%) and 4‘- O-β-maltotrioside (25%), by further CGTase-catalyzed glycosylation. Curcumin 4‘- O-β-glycosides showed suppressive action on IgE antibody formation and inhibitory effects on histamine release from rat peritoneal mast cells.

scholarly journals Kinetic analysis of the interaction of alkyl glycosides with two human β-glucosidases

1989 ◽  
Vol 262 (2) ◽  
pp. 541-548 ◽  
Author(s):  
V Gopalan ◽  
L B Daniels ◽  
R H Glew ◽  
M Claeyssens
Keyword(s):  
Active Site ◽  
Alkyl Chain ◽  
Physiological Function ◽  
Alkyl Chain Length ◽  
Alkyl Glycosides ◽  
Structural Nature ◽  
Similarities And Differences ◽  
Beta Glucosidase ◽  
Free Energy Of Binding ◽  
Physiological Substrates

This paper addresses the similarities and differences in the topology of the catalytic centres of human liver cytosolic beta-glucosidase and placental lysosomal glucocerebrosidase, and utilizes well-documented reversible active-site-directed inhibitors. This comparative kinetic study was performed mainly to decipher the chemical and structural nature of the active site of the cytosolic beta-glucosidase, whose physiological function is unknown. Specifically, analysis of the effects of a family of alkyl beta-glucosides consistently displayed 100-250-fold lower inhibition constants with the cytosolic broad-specificity beta-glucosidase compared with the placental glucocerebrosidase; for example, with octyl beta-D-glucoside the Ki values were 10 microM and 1490 microM for the cytosolic and lysosomal beta-glucosidases respectively. Furthermore the higher affinity of the cytosolic beta-glucosidase than glucocerebrosidase for the amphipathic alkyl beta-D-glucosides was validated by the greater increase in the free energy of binding with increasing alkyl chain length [delta delta G0 (K,)/CH2: lysosomal enzyme, 2.01 kJ/mol (480 cal/mol); cytosolic enzyme, 3.05 kJ/mol (730 cal/mol)]. The implications of the presence of highly non-polar domains in the active site of the cytosolic beta-glucosidase are discussed with regard to its potential physiological substrates.

Sign in / Sign up

Export Citation Format

Share Document