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Maltopentaose

$78

  • Brand : BIOFRON

  • Catalogue Number : BF-M1002

  • Specification : 98%

  • CAS number : 34620-76-3

  • Formula : C30H52O26

  • Molecular Weight : 828.72

  • PUBCHEM ID : 124005

  • Volume : 20mg

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Catalogue Number

BF-M1002

Analysis Method

HPLC,NMR,MS

Specification

98%

Storage

-20℃

Molecular Weight

828.72

Appearance

White crystalline powder

Botanical Source

glucose

Structure Type

Others

Category

Standards;Natural Pytochemical;API

SMILES

C(C1C(C(C(C(O1)OC2C(OC(C(C2O)O)OC3C(OC(C(C3O)O)OC4C(OC(C(C4O)O)OC(C(CO)O)C(C(C=O)O)O)CO)CO)CO)O)O)O)O

Synonyms

6-{[6-{[6-({4,5-Dihydroxy-2-(hydroxymethyl)-6-[2,3,4-trihydroxy-1-(hydroxymethoxy)butoxy]tetrahydro-2H-pyran-3-yl}oxy)-2,4,5-trihydroxytetrahydro-2H-pyran-3-yl]oxy}-4,5-dihydroxy-2-(hydroxymethyl)tetrahydro-2H-pyran-3-yl]oxy}tetrahydro-2H-pyran-2,3,4,5-tetrol/MALTOHEXAOSERESEARCH GRADE/malto-hexaose/MALTOPENTAOSE/Amylopentaose/Maltohexose/malto-pentaose/Maltohexaose,tech./Glc6/maltohexanose,dp6/AMYLOHEXAOSE

IUPAC Name

(2R,3R,4R,5R)-4-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-3,4-dihydroxy-6-(hydroxymethyl)-5-[(2R,3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-2,3,5,6-tetrahydroxyhexanal

Density

1.9±0.1 g/cm3

Solubility

Flash Point

709.1±34.3 °C

Boiling Point

1248.9±65.0 °C at 760 mmHg

Melting Point

InChl

InChl Key

WGK Germany

RID/ADR

HS Code Reference

2940000000

Personal Projective Equipment

Correct Usage

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

Meta Tag

provides coniferyl ferulate(CAS#:34620-76-3) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

PMID

31896254

Abstract

Maltooligosaccharide-forming amylases (MFAses) are promising tools for a variety of food industry applications because they convert starch into functional maltooligosaccharides. The MFAse from Bacillus stearothermophilus STB04 (BstMFAse) is a thermostable enzyme that preferentially produces maltopentaose and maltohexaose. An X-ray crystal structure of the BstMFAse-acarbose complex suggested that mutation of glycine 109 would increase its maltohexaose specificity. Using site-directed mutagenesis, glycine 109 was replaced with several different amino acids. Mutant-containing asparagine (G109N), aspartic acid (G109D), and phenylalanine (G109F) produced 36.1, 42.4, and 39.0% maltohexaose from starch, respectively, which was greater than that produced by the wild-type (32.9%). These mutants also exhibited substantially altered oligosaccharide hydrolysis patterns in favor of maltohexaose production. Homology models suggested that the mutants form extra interactions with the substrate at subsite -6, which were responsible for the enhanced maltohexaose specificity of BstMFAse. The results of this study support the proposition that binding of the substrate’s nonreducing end in the nonreducing end-subsite of the MFAse active center plays a crucial role in its product specificity.

KEYWORDS

crystal structure; maltohexaose; maltooligosaccharide-forming amylase; oligosaccharide hydrolysis pattern; product specificity

Title

Structure-Based Engineering of a Maltooligosaccharide-Forming Amylase To Enhance Product Specificity.

Author

Xie X1, Ban X1, Gu Z2,1,3, Li C2,1,3, Hong Y2,1,3, Cheng L2,1,3, Li Z2,1,3.

Publish date

2020 Jan 22

PMID

31442704

Abstract

Tropomyosin (TM) is the main allergen of shrimp. Glycation reportedly reduced the allergenicity of TM, and the allergenicity reduction was heavily dependent upon the sources of saccharides. In this work we investigated, how glycation of tropomyosin by functional oligosaccharides affected the allergenicity. Compared to TM, the TM glycated by galacto-oligosaccharide (TM-GOS), mannan-oligosaccharide (TM-MOS) and maltopentaose (TM-MPS) had lower allergenicity and induced weaker mouse allergy responses. While the TM glycated by fructo-oligosaccharide (TM-FOS) had stronger allergenicity and induced severe mouse allergy symptoms, due to the generation of neoallergns that belonged to advanced glycation end products (e.g. CML). Therefore, GOS, MOS and MPS could be applied to desensitize shrimp TM-induced food allergy through glycation, while FOS was not suitable to reduce TM allergenicity. Glycation of TM by GOS, MOS and MPS, especially for MPS, significantly reduced allergenicity and alleviated allergy symptoms, which could be potentially explored for immunotherapy for shrimp-allergic patients.

Copyright © 2019 Elsevier Ltd. All rights reserved.

KEYWORDS

Advanced glycation end products; Allergenicity; Functional oligosaccharide; Glycation; N(ɛ)-(carboxymethyl) lysine; Tropomyosin

Title

Insight into the allergenicity of shrimp tropomyosin glycated by functional oligosaccharides containing advanced glycation end products.

Author

Zhang Z1, Li XM2, Xiao H3, Nowak-Wegrzyn A4, Zhou P5.

Publish date

2020 Jan 1

PMID

30902292

Abstract

The allergenicity suppression of tropomyosin (TM) from Exopalaemon modestus by glycation with saccharides of different molecular sizes (glucose, maltose, maltotriose, maltopentaose and maltoheptaose) was investigated using immunoblotting, human colon epithelial cell line (Caco-2) and human basophil cell line (KU812). Glycation of TM by glucose, maltotriose, maltopentaose and maltoheptaose significantly destructed and masked TM epitopes to obtain lower allergenicity, while glycation of TM by maltose had insignificant suppression on TM allergenicity. In addition, the glycated TM by glucose, maltotriose, maltopentaose and maltoheptaose inhibited the proliferation and IL-8 secretion of Caco-2, and the CD63 and CD203c expression, MAPK signaling of KU812 basophils, while the glycated TM by maltose had insignificant suppression on the allergy reactivities of Caco-2 cells and KU812 basophils. Glycation of TM by saccharides with larger molecular sizes (such as maltoheptaose) could provide new insight into the desensitization of shrimp-induced food allergy.

Copyright © 2019 Elsevier Ltd. All rights reserved.

KEYWORDS

Allergenicity; Caco-2; Exo m 1; Exopalaemon modestus; Glycation; KU812 basophil; Tropomyosin

Title

Allergenicity suppression of tropomyosin from Exopalaemon modestus by glycation with saccharides of different molecular sizes.

Author

Zhang Z1, Xiao H2, Zhou P3.

Publish date

2019 Aug 1


Description :

Maltopentaose is the shortest chain oligosaccharide that can be classified as maltodextrin and is also used in a study to investigate glycation and phosphorylation of α-lactalbumin.