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|Stability:||> 10 years under recommended storage conditions|
|Synonyms:||Borohydride reduced 63-α-D-maltotriosyl-maltotriose|
|Substrate For (Enzyme):||Amyloglucosidase, Isopullulanase, Neopullulanase, Pullulanase/Limit-Dextrinase|
High purity 63-α-D-maltotriosyl-maltotriitol for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This compound can be used as a substrate for the characeterisation of pullulanase or limit dextrinase enzymes using a reducing sugar method (e.g. Nelson-Somogyi). The borohydride reduced analogue is used in place of 63-α-D-maltotriosyl-maltotriose (Cat. No. O-MTMT), because being a reducing sugar itself, the native oligosaccharide generates a large ‘blank’ value in this assay.
Glycerol Free E-AMGDFPD - Amyloglucosidase (Aspergillus niger) Powder E-AMGFR-100MG - Amyloglucosidase (Aspergillus niger) E-AMGPU - Amyloglucosidase (Rhizopus sp.) E-TSAGL - α-Glucosidase (Bacillus stearothermophilus) E-TSAGS - α-Glucosidase (Bacillus stearothermophilus) (Recombinant) E-MALTS - α-Glucosidase (yeast maltase) E-TRNGL - α-Glucosidase (Aspergillus niger) E-OAGUM - Oligo-α-1,6-Glucosidase (microbial) E-MALBS - Oligo-α-(1,4-1,6)-glucosidase (Bacillus sp.) E-ISPUAN - Isopullulanase (Aspergillus niger) E-GAMP - Glucoamylase P (H. resinae)
McCleary, B. V., Mangan, D., McKie, V., Cornaggia, C., Ivory, R. & Rooney, E. (2014). Carbohydrate Research, 393, 60-69.
Specific and highly sensitive colourimetric and fluorometric substrate mixtures have been prepared for the measurement of pullulanase and limit-dextrinase activity and assays employing these substrates have been developed. These mixtures comprise thermostable α- and β-glucosidases and either 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-maltotriosyl (1-6) α-maltotrioside (BzCNPG3G3, 1) as a colourimetric substrate or 4,6-O-benzylidene-4-methylumbelliferyl-β-maltotriosyl (1-6) α-maltotrioside (BzMUG3G3, 2) as a fluorometric substrate. Hydrolysis of substrates 1 and 2 by exo-acting enzymes such as amyloglucosidase, β-amylase and α-glucosidase is prevented by the presence of the 4,6-O-benzylidene group on the non-reducing end D-glucosyl residue. The substrates are not hydrolysed by any α-amylases studied, (including those from Aspergillus niger and porcine pancreas) and are resistant to hydrolysis by Pseudomonas sp. isoamylase. On hydrolysis by pullulanase, the 2-chloro-4-nitrophenyl-β-maltotrioside (3) or 4-methylumbelliferyl-β-maltotrioside (4) liberated is immediately hydrolysed to D-glucose and 2-chloro-4-nitrophenol or 4-methylumbelliferone. The reaction is terminated by the addition of a weak alkaline solution leading to the formation of phenolate ions in solution whose concentration can be determined using either spectrophotometric or fluorometric analysis. The assay procedure is simple to use, specific, accurate, robust and readily adapted to automation.Hide Abstract