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Raffinose

$52

  • Brand : BIOFRON

  • Catalogue Number : BD-P0661

  • Specification : 98.0%(HPLC)

  • CAS number : 512-69-6

  • Formula : C18H32O16

  • Molecular Weight : C18H32O16

  • Volume : 25mg

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Catalogue Number

BD-P0661

Analysis Method

Specification

98.0%(HPLC)

Storage

2-8°C

Molecular Weight

C18H32O16

Appearance

Botanical Source

Structure Type

Carbohydrates

Category

SMILES

C(C1C(C(C(C(O1)OCC2C(C(C(C(O2)OC3(C(C(C(O3)CO)O)O)CO)O)O)O)O)O)O)O

Synonyms

(2R,3R,4S,5S,6R)-2-{[(2S,3S,4S,5R)-3,4-Dihydroxy-2,5-bis(hydroxymethyl)tetrahydro-2-furanyl]oxy}-6-({[(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl]oxy}methyl)tetrahydro-2H-pyran-3,4,5-triol/β-D-Fructofuranosyl-α-D-galactopyranosyl-(1->6)-α-D-glucopyranoside/Gossypose/α-D-Glucopyranoside, β-D-fructofuranosyl O-α-D-galactopyranosyl-(1->6)-/MELITRIOSE/Raffinose/β-D-Fructofuranosyl α-D-galactopyranosyl-(1->6)-α-D-glucopyranoside/b-D-Fructofuranosyl-O-a-D-galactopyranosyl-(1®6)-a-D-glucopyranoside/Melitose/Raffinose (8CI)/D-(+)-Raffinose

IUPAC Name

Applications

Density

1.8±0.1 g/cm3

Solubility

Carbohydrates

Flash Point

488.9±34.3 °C

Boiling Point

884.8±65.0 °C at 760 mmHg

Melting Point

80ºC

InChl

InChl Key

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:512-69-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

31710929

Abstract

Autophagy is an important process for maintaining intracellular homeostasis. Our previous study demonstrated that autophagy was down-regulated in ultraviolet B (UVB)-irradiated keratinocytes. Raffinose is a natural oligosaccharide that serves as a novel activator of autophagy and as a balancing agent to regulate the diversity of environmental stress. However, whether raffinose balances ultraviolet stress through the autophagy activation pathway has yet to be established. In this study, we found that raffinose treatment inhibited the LDH release and trypan blue staining in UVB-challenged human keratinocytes cell line HaCaT but did not affect the cleavage of apoptotic markers Caspase-3 and PARP, as well as translocation into nucleus of other cell death markers Endonuclease G and AIF. Moreover, we confirmed that raffinose treatment enhanced autophagy flux in an MTOR-independent manner in HaCaT cells. Importantly, decrease of LC3-II turnover in UVB-irradiated keratinocytes could be rescued by raffinose treatment, indicating that raffinose treatment increased autophagy in UVB-irradiated HaCaT cells. Furthermore, the effect on cell death by raffinose was inhibited when autophagy was suppressed with either a small interfering RNA targeting ATG5 (siATG5) or autophagic inhibitor wortmannin. In conclusion, we demonstrated that raffinose increases MTOR-independent autophagy and reduces cell death in UVB-irradiated keratinocytes. Our study indicated that the natural agent raffinose presents the potential value in opposing photodamage.

Copyright © 2019 Elsevier B.V. All rights reserved.

KEYWORDS

Autophagy; Cell death; Keratinocyte; Raffinose; Ultraviolet

Title

Raffinose increases autophagy and reduces cell death in UVB-irradiated keratinocytes.

Author

Lin S1, Li L1, Li M1, Gu H2, Chen X3.

Publish date

2019 Dec;

PMID

31601209

Abstract

BACKGROUND:
α-Galactosidases are enzymes that act on galactosides present in many vegetables, mainly legumes and cereals, have growing importance with respect to our diet. For this reason, the use of their catalytic activity is of great interest in numerous biotechnological applications, especially those in the food industry directed to the degradation of oligosaccharides derived from raffinose. The aim of this work has been to optimize the recombinant production and further characterization of α-galactosidase of Saccharomyces cerevisiae.

RESULTS:
The MEL1 gene coding for the α-galactosidase of S. cerevisiae (ScAGal) was cloned and expressed in the S. cerevisiae strain BJ3505. Different constructions were designed to obtain the degree of purification necessary for enzymatic characterization and to improve the productive process of the enzyme. ScAGal has greater specificity for the synthetic substrate p-nitrophenyl-α-D-galactopyranoside than for natural substrates, followed by the natural glycosides, melibiose, raffinose and stachyose; it only acts on locust bean gum after prior treatment with β-mannosidase. Furthermore, this enzyme strongly resists proteases, and shows remarkable activation in their presence. Hydrolysis of galactose bonds linked to terminal non-reducing mannose residues of synthetic galactomannan-oligosaccharides confirms that ScAGal belongs to the first group of α-galactosidases, according to substrate specificity. Optimization of culture conditions by the statistical model of Response Surface helped to improve the productivity by up to tenfold when the concentration of the carbon source and the aeration of the culture medium was increased, and up to 20 times to extend the cultivation time to 216 h.

CONCLUSIONS:
ScAGal characteristics and improvement in productivity that have been achieved contribute in making ScAGal a good candidate for application in the elimination of raffinose family oligosaccharides found in many products of the food industry.

KEYWORDS

Biochemical characterization; Production optimization; Raffinose family oligosaccharides; Saccharomyces cerevisiae; α-Galactosidase

Title

Optimization of Saccharomyces cerevisiae α-galactosidase production and application in the degradation of raffinose family oligosaccharides.

Author

alvarez-Cao ME1, Cerdan ME1, Gonzalez-Siso MI1, Becerra M2.

Publish date

2019 Oct 10

PMID

31494392

Abstract

HYPOTHESIS:
The development of functional and nutritional surfactants for the food industry remains a subject of great interest. Herein, therefore, we report on the design and synthesis of novel trisaccharide (raffinose) monoester-based surfactants in the expectation that they would display functional properties superior to certain disaccharide-based, commercially-deployed emulsifiers and thus have potential for industrial applications.

EXPERIMENTS:
The title esters were prepared by enzymatic methods and their properties as surfactants evaluated through determination of their HLB values, water solubilities, CMCs, foamabilities and foaming stabilities as well as through investigation of their impacts on the stability of oil-in-water emulsions over a range of storage times and under certain other conditions.

FINDINGS:
The emulsifying properties of 6-O-acylraffinose esters are dictated, in large part, by the length of the associated alkyl chains. The results of storage and environmental stress experiments revealed that the increasing length of alkyl chains enhances the stability of the derived emulsions. All the raffinose ester-stabilized oil-in-water emulsions displayed stratification effects under strongly acidic conditions (pH ≤ 4) or at high ionic strength (≥300 mM) while possessing reasonable resistance to variations in temperature. As such, a number of the raffinose monoesters showed greater stability to environmental stress than their commercially-deployed and sucrose-based counterparts. The structure-property profiles established through the present study provide a definitive guide for the development of raffinose esters as novel emulsifiers, particularly in the food industry.

Copyright © 2019 Elsevier Inc. All rights reserved.

KEYWORDS

Emulsifying potency; Foaming property; Food emulsifiers; Raffinose monoesters; Structure-property profile; Surface-active property

Title

Fatty acid ester surfactants derived from raffinose: Synthesis, characterization and structure-property profiles.

Author

Li X1, Hai YW1, Ma D1, Chen J2, Banwell MG3, Lan P4.

Publish date

2019 Nov 15