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By Leticia Casas-Godoy, Sophie Duquesne, Florence Bordes, Georgina Sandoval, Alain Marty (auth.), Georgina Sandoval (eds.)
Lipases are the main utilized enzymes in natural synthesis because of their vast substrate reputation and thanks to the supply of the molecular, biochemical, themodynamical and solvent engineering instruments, which permits the optimization of lipases and lipase-catalyzed reactions. nevertheless, phospholipases are rising as precious enzymes in nutrition and pharmaceutical industries. In Lipases and Phospholipases: equipment and Protocols, specialist researchers within the box offer key thoughts to enquire those crucial enzymes. concentrating on primary matters, present and new functions in addition to useful step by step protocols, and the broad purposes of lipases and the aptitude software of phospholipases and its inhibitors. Written within the hugely winning Methods in Molecular Biology™ sequence structure, the chapters contain the type of unique description and implementation suggestion that's an important for purchasing optimum ends up in the laboratory.
Thorough and intuitive, Lipases and Phospholipases: Methods and Protocols aids scientists in carrying on with to review lipases, phopholipases and comparable enzymes.
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Extra info for Lipases and Phospholipases: Methods and Protocols
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Accessed Nov 2010 Freedonia (2009) World Enzymes Market. Report Linker. html . Accessed Nov 2010 Freedonia (2010) Enzymes. pdf. Accessed Nov 2010 Lipases: An Overview 27 102. Hasan F, Shah AA, Hameed A (2006) Industrial applications of microbial lipases. Enzyme Microb Technol 39:235–251 103. Aloulou A, Rodriguez JA, Puccinelli D et al (2007) Purification and biochemical characterization of the LIP2 lipase from Yarrowia lipolytica. Biochim Biophys Acta 1771: 228–237 104. Houde A, Kademi A, Leblanc D (2004) Lipases and their industrial applications.
This selectivity also refers to the preference of lipases toward short-, medium-, or long-chain fatty acids and to the degree of unsaturation and potential substitutions of the substrate. The preference of a lipase for acyl groups of different sizes is directly influenced by the shape of its binding site, and the nature of the amino acids composing this binding site. Indeed, the very homologous C. rugosa lipase isoforms differ in chain length specificity due to slight modifications of the amino acids in their tunnel-shaped binding site (87).
Sommadelpero C, Valette A, Lepetitthevenin J et al (1995) Purification and properties of a monoacylglycerol lipase in human erythrocytes. Biochem J 312:519–525 87. Lopez N, Pernas MA, Pastrana LM et al (2004) Reactivity of pure Candida rugosa lipase isoenzymes (Lip1, Lip2, and Lip3) in aqueous and organic media. Influence of the isoenzymatic profile on the lipase performance in organic media. Biotechnol Prog 20:65–73 88. Horchani H, Ben Salem N, Chaari A et al (2010) Staphylococcal lipases stereoselectively 1 89.