13382-86-0

Basic information

• Product Name: manninotriose
• Synonyms: manninotriose;6-O-[6-O-(α-D-Galactopyranosyl)-α-D-galactopyranosyl]-D-glucose;O-alpha-D-Galactopyranosyl-(1-6)-O-alpha-D-galactopyranosyl-(1-6)-D-glucose
• CAS NO: 13382-86-0
• Molecular Formula: C₁₈H₃₂O₁₆
• Molecular Weight: 504.43708
• Mol File: 13382-86-0.mol
• Article Data: 5

Chemical Properties

• Boiling Point: 968.5°Cat760mmHg
• Flash Point: 332.9°C
• Appearance: /
• Density: 1.75g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.651
• Storage Temp.: 2-8°C
• PKA: 12.45±0.20(Predicted)
• CAS DataBase Reference: manninotriose(CAS DataBase Reference)
• NIST Chemistry Reference: manninotriose(13382-86-0)
• EPA Substance Registry System: manninotriose(13382-86-0)

Safety Data

• Hazardous Substances Data: 13382-86-0(Hazardous Substances Data)

Usage

General Description

Manninotriose is a trisaccharide composed of three sugar units: D-mannose, D-glucose, and D-mannose. It is commonly found in the cell walls of certain fungi and has been identified as a component of the polysaccharides in the cell walls of several yeast and mold species. Manninotriose has also been found to have potential health benefits, including anti-inflammatory and immunomodulatory properties. Additionally, it has been proposed as a potential prebiotic, promoting the growth of beneficial gut bacteria. Research on the potential uses and benefits of manninotriose is ongoing, and further studies are needed to fully understand its biological activities and potential applications.

InChI:InChI=1/C18H32O16/c19-1-5(21)9(23)10(24)6(22)3-31-17-16(30)14(28)12(26)8(34-17)4-32-18-15(29)13(27)11(25)7(2-20)33-18/h1,5-18,20-30H,2-4H2/t5-,6+,7+,8+,9+,10+,11-,12-,13-,14-,15+,16+,17-,18-/m0/s1

Upstream product

• 69-79-4 D-maltose 
• 499-40-1 melibiose 

Relevant articles and documents

Heterologous expression of a thermostable α-glucosidase from Geobacillus sp. Strain HTA-462 by Escherichia coli and its potential application for isomaltose–oligosaccharide synthesis

Isomaltose–oligosaccharides (IMOs), as food ingredients with prebiotic functionality, can be prepared via enzymatic synthesis using α-glucosidase. In the present study, the α-glucosidase (GSJ) from Geobacillus sp. strain HTA-462 was cloned and expressed in Escherichia coli BL21 (DE3). Recombinant GSJ was purified and biochemically characterized. The optimum temperature condition of the recombinant enzyme was 65 ?C, and the half-life was 84 h at 60 ?C, whereas the enzyme was active over the range of pH 6.0–10.0 with maximal activity at pH 7.0. The α-glucosidase activity in shake flasks reached 107.9 U/mL and using 4-Nitrophenyl β-D-glucopyranoside (pNPG) as substrate, the Km and Vmax values were 2.321 mM and 306.3 U/mg, respectively. The divalent ions Mn2+ and Ca2+ could improve GSJ activity by 32.1% and 13.8%. Moreover, the hydrolysis ability of recombinant α-glucosidase was almost the same as that of the commercial α-glucosidase (Bacillus stearothermophilus). In terms of the transglycosylation reaction, with 30% maltose syrup under the condition of 60 ?C and pH 7.0, IMOs were synthesized with a conversion rate of 37%. These studies lay the basis for the industrial application of recombinant α-glucosidase.

Heterologous expression and biochemical characterization of α-glucosidase from aspergillus niger by pichia pastroris

The aglu of Aspergillus niger encodes the pro-protein of α-glucosidase, and the mature form of wild-type enzyme is a heterosubunit protein. In the present study, the cDNA of α-glucosidase was cloned and expressed in Pichia pastoris strain KM71. The activity of recombinant enzyme in a 3 L fermentor reached 2.07 U/mL after 96 h of induction. The recombinant α-glucosidase was able to produce oligoisomaltose. The molecular weight of the recombinant enzyme was estimated to be about 145 kDa by SDS-PAGE, and it reduced to 106 kDa after deglycosylation. The enzymatic activity of recombinant α-glucosidase was not significantly affected by a range of metal ions. The optimum temperature of the enzyme was 60 °C, and it was stable below 50 °C. The enzyme was active over the range of pH 3.0-7.0 with maximal activity at pH 4.5. Using pNPG as substrate, the Km and Vmax values were 0.446 mM and 43.48 U/mg, respectively. These studies provided the basis for the application of recombinant α-glucosidase in the industry of functional oligosaccharides.

Research on the strong transglycosylation activity in Aspergillus niger

Aspergillus niger M-1 strain shows strong transglycosylation activity. A gene of it was introduced into Escherichia coli, and isomalto-oligosaccharides were isolated by a chemical enzymatic method in order to measure the transglycosylation activity.