Prices exclude VAT
Available for shipping
|Content:||250 mg or 1 g|
|Storage Temperature:||Below -10oC|
|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)
Li, X., Zhao, J., Fu, J., Pan, Y., & Li, D. (2018). International Journal of Biological Macromolecules, In Press.
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