Esterase from Pseudomonas fluorescens

<strong>Esterase from Pseudomonas fluorescens</strong>_x000D_ <strong>Catalog number:</strong> B2013857_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 10 mg_x000D_ <strong>Molecular Weight or Concentration:</strong>_x000D_ ≥4 U/mg_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> 2-8°C_x000D_ <strong>Keywords:</strong> Carboxylic ester hydrolase_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: 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_ <a href="https://pubmed.ncbi.nlm.nih.gov/23143253">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. </a>_x000D_ _x000D_ <strong>Products Related to Esterase from Pseudomonas fluorescens can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>