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Publisher Summary A central question that can be addressed using structural data is whether or not—and if so to what extent—lipases bind to, react with, or are activated by lipid-water interfaces. The fact that water-soluble lipases are able to hydrolyze poorly water-soluble substrates requires carefully controlled assay conditions. These are essential before detailed understanding of structure-function relations can be obtained from such kinetic and mechanistic studies. This chapter describes methods that can be applied to achieve this goal. Industrially applied lipases are mainly obtained from microbial sources. Application of protein-engineering techniques has widened the range of lipases to choose from considerably. The inaccessible active site in many lipases, including that of Pseudomonas glumae lipase, adds further complexity. In contrast, lipolytic enzymes do exist, for example, Fusarium solani pisi cutinase, that have an exposed active site, but still show behavior also noted for the more complex lipases. The structure and function of these two lipases are discussed in the chapter. |
