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Nergy 2013, 50:42732. Sakakibara M, Wang D, Takahashi R, Takahashi K, Mori S: Influence of ultrasound irradiation on hydrolysis of sucrose catalyzed by invertase. Enzyme Microbiol Technol 1996, 18:44448. Brenelli ECS, Fernandes JLN: Stereoselective acylations of 1,2-azidoalcohols with vinyl acetate, catalyzed by lipase Amano PS. Tetrahedron: Asymmetry 2003, 14:1255259. Martins AB, Graebin GN, Lorenzoni ASG, Lafuente RF, Rodrigues RC: Rapid and higher yields of synthesis of butyl acetate catalyzed by Novozym 435: reaction optimization by response surface methodology. Process Biochem 2011, 46:2311316. Veljkovi VB, Avramovi JM, Stamenkovi OS: Biodiesel production by Bak site Ultrasound-assisted transesterification: State in the art as well as the perspectives. Renew Sustain Energy Rev 2012, 16:1193209. Yadav GD, Lathi PS: Synthesis of citronellol laurate in organic media catalyzed by immobilized lipase: kinetic research. J Mol Catal B Enzym 2004, 27:11319.Cui et al. Chemistry Central Journal 2013, 7:180 http:journal.chemistrycentralcontent71Page ten of29. Bezbradica D, Mijin D, Marinkovi S, Knezevi Z: The Candida rugosa lipase catalyzed synthesis of amyl isobutyrate in organic solvent and solvent no cost technique: a kinetic study. J Mol Catal B Enzym 2006, 38:116. 30. Zhang DH, Li YQ, Li C: Kinetics of enzymatic synthesis of L-ascorbyl acetate by Lipozyme TLIM and Novozym 435. Biotechnol Bioproc Eng 2012, 17:606. 31. Box GEP, Draper NR: Empirical Model-building and Response Surfaces. New York: Wiley; 1987.doi:ten.11861752-153X-7-180 Cite this short article as: Cui et al.: Ultrasound-assisted lipase-catalyzed synthesis of D-isoascorbyl palmitate: approach optimization and Kinetic evaluation. Chemistry Central Journal 2013 7:180.Publish with ChemistryCentral and just about every scientist can read your perform absolutely free of chargeOpen access provides possibilities to our colleagues in other components with the globe, by allowing everyone to view the content totally free of charge.W. Jeffery Hurst, The Hershey Enterprise. readily available free of charge for the complete scientific community peer reviewed and published instantly upon acceptance cited in PubMed and archived on PubMed Central yours you retain the copyrightSubmit your manuscript right here: http:chemistrycentralmanuscript
Author’s ChoiceTHE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 289, NO. five, pp. 2880 887, January 31, 2014 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Published inside the U.S.A.Crystal Structure from the Tetrameric Fibrinogen-like D4 Receptor site recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) ProteinReceived for publication, September 19, 2013, and in revised type, November 27, 2013 Published, JBC Papers in Press, November 28, 2013, DOI ten.1074jbc.M113.Annette K. Shrive1,2, Jesper B. Moeller, Ian Burns, Jenny M. Paterson, Amy J. Shaw, Anders Schlosser Grith L. Sorensen Trevor J. Greenhough, and Uffe HolmskovFrom the Analysis Institute of Science and Technology in Medicine, College of Life Sciences, Keele University, Staffordshire ST5 5BG, Uk and the �Department of Cardiovascular and Renal Investigation, Institute of Molecular Medicine, University of Southern Denmark, DK-5000 Odense, DenmarkBackground: FIBCD1 is usually a tetrameric plasma membrane protein that makes use of a fibrinogen-like recognition domain (FReD) for pattern recognition of acetyl groups on chitin. Results: The x-ray structure of the FIBCD1 FReD reveals how FIBCD1 binds acetylated and sulfated molecules. Conclusion: FReD domains combine versatility with conservation to recog.
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