Esterase from Pseudomonas fluorescens

• Short Description:

  Catalog Number: B2013857 (10 mg)_x000D_ Esterase from Pseudomonas fluorescens is a high quality Esterase from Pseudomonas fluorescens, recombinant from E. coli. This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request._x000D_ _x000D_

• Description:

  Esterase from Pseudomonas fluorescens_x000D_ Catalog number: B2013857_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 10 mg_x000D_ Molecular Weight or Concentration:_x000D_ ‰¥4 U/mg_x000D_ Supplied as: Powder_x000D_ Applications: molecular tool for various biochemical applications_x000D_ Storage: 2-8°C_x000D_ Keywords: Carboxylic ester hydrolase_x000D_ Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ References:_x000D_ 1: Martins ML, Pinto UM, Riedel K, Vanetti MC. Milk-deteriorating exoenzymes from Pseudomonas fluorescens 041 isolated from refrigerated raw milk Braz J Microbiol. 2015 Mar 31;46(1):207-17._x000D_ 2: Krebsf_nger N, Schierholz K, Bornscheuer UT. Enantioselectivity of a recombinant esterase from Pseudomonas fluorescens towards alcohols and carboxylic acids J Biotechnol. 1998 Feb 5;60(1-2):105-11._x000D_ 3: Ferreira LM, Wood TM, Williamson G, Faulds C, Hazlewood GP, Black GW, Gilbert HJ. A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain Biochem J. 1993 Sep 1;294 ( Pt 2)(Pt 2):349-55._x000D_ 4: Matrawy AA, Khalil AI, Embaby AM. Molecular study on recombinant cold-adapted, detergent- and alkali stable esterase (EstRag) from Lysinibacillus sp.: a member of family VI World J Microbiol Biotechnol. 2022 Sep 7;38(12):217._x000D_ 5: Bartolom B, Faulds CB, Kroon PA, Waldron K, Gilbert HJ, Hazlewood G, Williamson G. An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (Xy1D) release a 5-5' ferulic dehydrodimer (diferulic acid) from barley and wheat cell walls Appl Environ Microbiol. 1997 Jan;63(1):208-12._x000D_ 6: Schliessmann A, Hidalgo A, Berenguer J, Bornscheuer UT. Increased enantioselectivity by engineering bottleneck mutants in an esterase from Pseudomonas fluorescens Chembiochem. 2009 Dec 14;10(18):2920-3._x000D_ 7: Choi KD, Jeohn GH, Rhee JS, Yoo OJ. Cloning and nucleotide sequence of an esterase gene from Pseudomonas_fluorescens and expression of the gene in Escherichia coli Agric Biol Chem. 1990 Aug;54(8):2039-45._x000D_ 8: Liu W, Li M, Yan Y. Heterologous expression and characterization of a new lipase from Pseudomonas_fluorescens Pf0-1 and used for biodiesel production Sci Rep. 2017 Nov 16;7(1):15711._x000D_ 9: Prim N, Bofill C, Pastor FI, Diaz P. Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes Biochimie. 2006 Jul;88(7):859-67._x000D_ 10: Kim S, Ngo TD, Kim KK, Kim TD. Characterization, crystallization and preliminary X-ray diffraction analysis of an (S)-specific esterase (pfEstA) from Pseudomonas fluorescens KCTC 1767: enantioselectivity for potential industrial applications Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1374-7. _x000D_ _x000D_ Products Related to Esterase from Pseudomonas fluorescens can be found at Enzymes

• Weight:

  0.15

• Length:

  2

• Width:

  0.5

• Height :

  0.5