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|Content:||250 mg or 1 g|
|Storage Temperature:||Below -10oC or Ambient|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||Amyloglucosidase|
High purity Panose for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Panose is formed by the action of neopullulanase on pullulan. It can be used as an analytical standard or as a substrate to help characterise the activities of other starch degrading enzymes including α-glucosidase and amyloglucosidase.
Data booklets for each pack size are located in the Documents tab.
Glycerol Free E-AMGDFPD - Amyloglucosidase (Aspergillus niger) Powder E-AMGFR-100MG - Amyloglucosidase (Aspergillus niger) E-AMGPU - Amyloglucosidase (Rhizopus sp.) E-GAMP - Glucoamylase P (H. resinae) 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-PULKP - Pullulanase M1 (Klebsiella planticola)
In vitro digestibility of commercial and experimental isomalto-oligosaccharides.
Hu, Y., Winter, V. & Gänzle, M. (2020). Food Research International, 134, 109250.
Isomalto-oligosaccharides (IMO) significantly contribute to the global oligosaccharide market. IMO are linear α-(1 → 6) linked oligosaccharides with isomaltotriose as the representative trisaccharide. Commercial IMO preparations ypically also contain panose-series oligosaccharides as a major component. In humans, IMO are partially digestible but the digestibility of specific components of commerical IMO preparations remains unknown. This study aimed to compare the in vitro digestibility of reference compounds, experimental α-gluco-oligosaccharides and commercial IMO. Experimental α-gluco-oligosaccharides were synthesized with the recombinant dextransucrase DsrM. Two in vitro digestion methods were used, a reference method matching the AOAC method for dietary fibre, and a protocol that uses brush border glycosyl hydrolases from the rat intestine. The α-gluco-oligosaccharides patterns after hydrolysis remain were analyzed by high performance anion exchange chromatography coupled to pulsed amperometric detection. Panose-series oligosaccharides were hydrolysed more rapidly by amylase and amyloglucosidase when compared to hydrolysis by rat intestinal enzymes. The rate of hydrolysis by rat intestinal enzymes decreased in the order panose > isomaltose, kojibiose or nigerose. Hydrolysis of panose-series oligosaccharides but not the hydrolysis of isomalto-oligosaccharides was dependent on the degree of polymerization. Qualitative analysis of oligosaccharides remaining after hydrolysis indicated that rat small intestinal enzymes hydrolyse their substrates from the non-reducing end. Taken together, results inform on the modification or optimization of current production processes for IMO to obtain tailored oligosaccharide preparations with reduced digestibility and an increased content of dietary fibre.Hide Abstract
Sequence analysis and biochemical properties of an acidophilic and hyperthermophilic amylopullulanase from Thermofilum pendens.
Li, X., Zhao, J., Fu, J., Pan, Y., & Li, D. (2018). International Journal of Biological Macromolecules, 114, 235-243.
The acidophilic and thermophilic pullulanases have many potential applications in the processes of starch liquefaction and saccharification. In this study, a gene encoding an amylopullulanase from Thermofilum pendens (TPApu) was heterologously expressed in Escherichia coli. Although TPApu possessed the same continuous GH57N_Apu domain and the succeeding α-helical region as other two amylopullulanases from Staphylothermus marinus (SMApu) and Caldivirga maquilingensis (CMApu), it only showed maximal amino acid identities of 25.7-28.7% with CMApu and SMApu. The purified TPApu appeared as a single band of SDS-PAGE with a molecular mass of 65.5 kDa and exhibited the maximal activity at pH 3.5 and 95-100°C. TPApu had the highest catalytic efficiency towards pullulan (kcat/km, 8.79 s-1 mL mg-1) and α-cyclodextrin (kcat/km, 0.36 s-1 mM-1). In the initial stages, the ring-opening reactions of γ-cyclodextrin, 6-O-glucosyl-β-cyclodextrin, 6-O-maltosyl-β-cyclodextrin and the debranching reactions of 6-O-maltooctaosyl-β-cyclodextrin were firstly catalyzed. In the subsequent reactions, a serial of maltooligosaccharides were produced. As the most acidophilic amylopullulanase among thermophilic pullulanases reported to date, TPApu preferred to debranch the DP6-12 side chains of amylopectin at pH 4.5 and 100°C.Hide Abstract