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Glucoamylase from Rhizopus

<strong>Glucoamylase from Rhizopus</strong>_x000D_ <strong>Catalog number:</strong> B2011027_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 5 g_x000D_ <strong>Molecular Weight or Concentration:</strong> na_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various chemical, biochemical and immunological applications_x000D_ <strong>Storage:</strong> 2-8°C_x000D_ <strong>Keywords:</strong> Acid Maltase from Rhizopus_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: Liu YN, Lai YT, Chou WI, Chang MD, Lyu PC. Solution structure of family 21 carbohydrate-binding module from Rhizopus oryzae glucoamylase Biochem J. 2007 Apr 1;403(1):21-30._x000D_ 2: Mertens JA, Skory CD. Isolation and characterization of two genes that encode active glucoamylase without a starch binding domain from Rhizopus oryzae Curr Microbiol. 2007 Jun;54(6):462-6._x000D_ 3: He Z, Zhang L, Mao Y, Gu J, Pan Q, Zhou S, Gao B, Wei D. Cloning of a novel thermostable glucoamylase from thermophilic fungus Rhizomucor pusillus and high-level co-expression with α-amylase in Pichia pastoris BMC Biotechnol. 2014 Dec 24;14:114._x000D_ 4: Takahashi T, Tsuchida Y, Irie M. Purification and some properties of three forms of glucoamylase from a Rhizopus species J Biochem. 1978 Nov;84(5):1183-94._x000D_ 5: Tang X, Luo T, Li X, Yang H, Yang Y, Li J, Xu B, Huang Z. Application and Analysis of Rhizopus oryzae Mycelia Extending Characteristic in Solid-state Fermentation for Producing Glucoamylase J Microbiol Biotechnol. 2018 Nov 28;28(11):1865-1875._x000D_ 6: Chu CH, Li KM, Lin SW, Chang MD, Jiang TY, Sun YJ. Crystal structures of starch binding domain from Rhizopus oryzae_glucoamylase in complex with isomaltooligosaccharide: insights into polysaccharide binding mechanism of CBM21 family Proteins. 2014 Jun;82(6):1079-85._x000D_ 7: Takahashi T, Kato K, Ikegami Y, Irie M. Different behavior towards raw starch of three forms of glucoamylase_from a Rhizopus sp J Biochem. 1985 Sep;98(3):663-71._x000D_ 8: Takegawa K, Kawasaki N, Iwahara S, Yamamoto K, Tochikura T, Mikami B, Morita Y. Primary structure of an N-linked sugar chain derived from glucoamylase of Rhizopus niveus Biochim Biophys Acta. 1989 Jan 27;990(1):98-100._x000D_ 9: Yang L, Dai X, Hou J, Ma C, Wang C, Wu Z, Li M. Construction of a Rhizopus arrhizus glucoamylase gene suitable for expression in distinct host: introns spliced artificially by PCR Mol Biol Rep. 2008 Mar;35(1):9-15._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/18588504">10: Tung JY, Chang MD, Chou WI, Liu YY, Yeh YH, Chang FY, Lin SC, Qiu ZL, Sun YJ. Crystal structures of the starch-binding domain from Rhizopus oryzae glucoamylase reveal a polysaccharide-binding path Biochem J. 2008 Nov 15;416(1):27-36. </a>_x000D_ _x000D_ <strong>Products Related to Glucoamylase from Rhizopus can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>

Product Specifications

Short Description

Catalog Number: B2011027 (5 g)

Weight

0.8

Length

2

Width

0.9

Height

0.9

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