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|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||Amyloglucosidase, β-Amylase|
High purity Maltotriose 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)
Measurement of Starch: Critical evaluation of current methodology.
McCleary, B. V., Charmier, L. M. J. & McKie, V. A. (2018). Starch‐Stärke, 71(1-2), 1800146.
Most commonly used methods for the measurement of starch in food, feeds and ingredients employ the combined action of α‐amylase and amyloglucosidase to hydrolyse the starch to glucose, followed by glucose determination with a glucose oxidase/peroxidase reagent. Recently, a number of questions have been raised concerning possible complications in starch analytical methods. In this paper, each of these concerns, including starch hydrolysis, isomerisation of maltose to maltulose, effective hydrolysis of maltodextrins by amyloglucosidase, enzyme purity and hydrolysis of sucrose and β‐glucans have been studied in detailed. Results obtained for a range of starch containing samples using AOAC Methods 996.11 and 2014 .10 are compared and a new simpler format for starch measurement is introduced. With this method that employs a thermostable α-amylase (as distinct from a heat stable α-amylase) which is both stable and active at 100°C and pH 5.0, 10 samples can be analysed within 2 h, as compared to the 6 h required with AOAC Method 2014.10.Hide Abstract
Characterization and engineering of two new GH9 and GH48 cellulases from a Bacillus pumilus isolated from Lake Bogoria.
Ogonda, L. A., Saumonneau, A., Dion, M., Muge, E. K., Wamalwa, B. M., Mulaa, F. J. & Tellier, C. (2021). Biotechnology Letters, 1-10.
Objectives: To search for new alkaliphilic cellulases and to improve their efficiency on crystalline cellulose through molecular engineering. Results: Two novel cellulases, BpGH9 and BpGH48, from a Bacillus pumilus strain were identified, cloned and biochemically characterized. BpGH9 is a modular endocellulase belonging to the glycoside hydrolase 9 family (GH9), which contains a catalytic module (GH) and a carbohydrate-binding module belonging to class 3 and subclass c (CBM3c). This enzyme is extremely tolerant to high alkali pH and remains significantly active at pH 10. BpGH48 is an exocellulase, belonging to the glycoside hydrolase 48 family (GH48) and acts on the reducing end of oligo-β1,4 glucanes. A truncated form of BpGH9 and a chimeric fusion with an additional CBM3a module was constructed. The deletion of the CBM3c module results in a significant decline in the catalytic activity. However, fusion of CBM3a, although in a non native position, enhanced the activity of BpGH9 on crystalline cellulose. Conclusions: A new alkaliphilic endocellulase BpGH9, was cloned and engineered as a fusion protein (CBM3a-BpGH9), which led to an improved activity on crystalline cellulose.Hide Abstract
The structure of the AliC GH13 α-amylase from Alicyclobacillus sp. reveals the accommodation of starch branching points in the α-amylase family.
Agirre, J., Moroz, O., Meier, S., Brask, J., Munch, A., Hoff, T., Anderson, C., Wilson, K. S. & Davies, G. J. (2019). Acta Crystallographica Section D: Structural Biology, 75(1), 1-7.
α-Amylases are glycoside hydrolases that break the α-1,4 bonds in starch and related glycans. The degradation of starch is rendered difficult by the presence of varying degrees of α-1,6 branch points and their possible accommodation within the active centre of α-amylase enzymes. Given the myriad industrial uses for starch and thus also for α-amylase-catalysed starch degradation and modification, there is considerable interest in how different α-amylases might accommodate these branches, thus impacting on the potential processing of highly branched post-hydrolysis remnants (known as limit dextrins) and societal applications. Here, it was sought to probe the branch-point accommodation of the Alicyclobacillus sp. CAZy family GH13 α-amylase AliC, prompted by the observation of a molecule of glucose in a position that may represent a branch point in an acarbose complex solved at 2.1 Å resolution. Limit digest analysis by two-dimensional NMR using both pullulan (a regular linear polysaccharide of α-1,4, α-1,4, α-1,6 repeating trisaccharides) and amylopectin starch showed how the Alicyclobacillus sp. enzyme could accept α-1,6 branches in at least the -2, +1 and +2 subsites, consistent with the three-dimensional structures with glucosyl moieties in the +1 and +2 subsites and the solvent-exposure of the -2 subsite 6-hydroxyl group. Together, the work provides a rare insight into branch-point acceptance in these industrial catalysts.Hide Abstract