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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||Amyloglucosidase, α-amylase, β-Amylase|
High purity Maltotetraose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
K-AMYLSD - α-Amylase SD Assay Kit R-AMGR3 - Amyloglucosidase Assay Reagent O-NAPC3-100 - β-Naphthyl-β-maltotrioside O-PNPC3-100 - 4-Nitrophenyl-β-maltotrioside O-BPNPC7 - Blocked 4-nitrophenyl-α-maltoheptaoside
Glycerol Free E-AMGDFPD - Amyloglucosidase (Aspergillus niger) Powder E-AMGFR-100MG - Amyloglucosidase (Aspergillus niger) E-TSAGL - α-Glucosidase (Bacillus stearothermophilus) E-TSAGS - α-Glucosidase (Bacillus stearothermophilus) (Recombinant) E-TRNGL - α-Glucosidase (Aspergillus niger) E-MAST - Malt Amylase Standard E-MASTP - Malt Amylase Standard (powder) E-MALAA - Maltogenic amylase (Bacillus sp.) E-OAGUM - Oligo-α-1,6-Glucosidase (microbial) E-MALBS - Oligo-α-(1,4-1,6)-glucosidase (Bacillus sp.) E-MALTS - α-Glucosidase (yeast maltase) E-AMGPU - Amyloglucosidase (Rhizopus sp.) E-GAMP - Glucoamylase P (H. resinae)
Starch digested product analysis by HPAEC reveals structural specificity of flavonoids in the inhibition of mammalian α-amylase and α-glucosidases.
Lim, J., Zhang, X., Ferruzzi, M. G. & Hamaker, B. R. (2019). Food Chemistry, 288, 413-421.
An accurate high-performance anion-exchange chromatography (HPAEC) method is presented to measure the inhibition property of flavonoids against mammalian starch digestive enzymes, because flavonoids interfere with commonly used 3,5-dinitrosalicylic acid (DNS) and glucose oxidase/peroxidase (GOPOD) methods. Eriodictyol, luteolin, and quercetin increased absorbance values (without substrate) in the DNS assay and, with substrate, either overestimated or underestimated values in the DNS and GOPOD assays. Using a direct HPAEC measurement method, flavonoids showed different inhibition properties against α-amylase and α-glucosidases, showing different inhibition constants (Ki) and mechanisms. The double bond between C2 and C3 on the C-ring of flavonoids appeared particularly important to inhibit α-amylase, while the hydroxyl group (OH) at C3 of the C-ring was related to inhibition of α-glucosidases. This study shows that direct measurement of starch digestion products by HPAEC should be used in inhibition studies, and provides insights into structure-function aspects of polyphenols in controlling starch digestion rate.Hide Abstract
Shao, Y. & Lin, A. H. M. (2017). Food Chemistry, 240, 898-903.
Measuring reducing sugar is a common practice in carbohydrate research, and the colorimetric assay developed by Somogyi and Nelson has a high sensitivity in a broad concentration range. However, the method is time-consuming when analyzing a large number of samples. In this study, a modified Somogyi-Nelson assay with excellent accuracy and sensitivity was developed using a 96-well microplate. This microassay greatly improves the analytic capacity and efficacy of the method.Hide Abstract