Maltogenic Amylase from Bacillus sp

<strong>Maltogenic Amylase from Bacillus sp</strong>_x000D_ <strong>Catalog number:</strong> B2014265_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 1 g_x000D_ <strong>Molecular Weight or Concentration:</strong> N/A_x000D_ <strong>Supplied as:</strong> Solid_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> Glucan 1,4-α-maltohydrolase, Maltogenic Amylase_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Mabrouk SB, Messaoud EB, Ayadi D, Jemli S, Roy A, Mezghani M, Bejar S. Cloning and sequencing of an original gene encoding a maltogenic amylase from Bacillus sp. US149 strain and characterization of the recombinant activity Mol Biotechnol. 2008 Mar;38(3):211-9._x000D_ 2: Jones A, Lamsa M, Frandsen TP, Spendler T, Harris P, Sloma A, Xu F, Nielsen JB, Cherry JR. Directed evolution of a maltogenic alpha-amylase from Bacillus sp. TS-25 J Biotechnol. 2008 Apr 30;134(3-4):325-33._x000D_ 3: Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH. Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other J Biol Chem. 2002 Jun 14;277(24):21891-7._x000D_ 4: Ben Mabrouk S, Ayadi-Zouari D, Ben Hlima H, Bejar S. Changes in the catalytic properties and substrate specificity of Bacillus sp. US149 maltogenic amylase by mutagenesis of residue 46 J Ind Microbiol Biotechnol. 2013 Sep;40(9):947-53._x000D_ 5: Ben Mabrouk S, Ayadi DZ, Ben Hlima H, Bejar S. Thermostability improvement of maltogenic amylase MAUS149 by error prone PCR J Biotechnol. 2013 Dec;168(4):601-6._x000D_ 6: Ben Mabrouk S, Aghajari N, Ben Ali M, Ben Messaoud E, Juy M, Haser R, Bejar S. Enhancement of the thermostability of the maltogenic amylase MAUS149 by Gly312Ala and Lys436Arg substitutions Bioresour Technol. 2011 Jan;102(2):1740-6._x000D_ 7: Kuchtov A, Janeek . Domain evolution in enzymes of the neopullulanase subfamily Microbiology (Reading). 2016 Dec;162(12):2099-2115._x000D_ 8: Kamasaka H, Sugimoto K, Takata H, Nishimura T, Kuriki T. Bacillus stearothermophilus neopullulanase selective hydrolysis of amylose to maltose in the presence of amylopectin Appl Environ Microbiol. 2002 Apr;68(4):1658-64._x000D_ 9: Li D, Park SH, Shim JH, Lee HS, Tang SY, Park CS, Park KH. In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase Carbohydr Res. 2004 Dec 6;339(17):2789-97._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/34427087">10: Te Poele EM, van der Hoek SE, Chatziioannou AC, Gerwig GJ, Duisterwinkel WJ, Oudhuis LAACM, Gangoiti J, Dijkhuizen L, Leemhuis H. GtfC Enzyme of Geobacillus sp. 12AMOR1 Represents a Novel Thermostable Type of GH70 4,6--Glucanotransferase That Synthesizes a Linear Alternating (1 6)/(1 4) -Glucan and Delays Bread Staling J Agric Food Chem. 2021 Sep 1;69(34):9859-9868. </a>_x000D_ _x000D_ <strong>Products Related to Maltogenic Amylase from Bacillus sp can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>