Lipolytic Enzymes focuses on the biochemistry of lipolytic enzymes, particularly, pancreatic lipase and phospholipase 2 as well as their structure and catalytic mechanism. It explores the kinetics of lipolysis, the digestive lipases of nonmammalian animals, the assay and purification of cholesterol esterases and phospholipases, the method phospholipases use in hydrolyzing phospholipids, and the adaptive mechanism of lipolytic enzymes at the lipid-water interface.
Organized into eight chapters, this book begins with an overview of the importance of lipolytic enzymes, including their medical, therapeutic, food, and other industrial applications. It then proceeds with a discussion on the classification of lipolytic enzymes according to the type of bond they hydrolyze and the substrates on which they act. The next chapters look at the substrates and supersubstrates of lipolytic enzymes, along with their maximal velocity and the Michaelis constant. Moreover, the book talks about the detection and assay of lipases, the molecular properties of pancreatic cholesterol esterases, the stimulating effect of bile salts on cholesterol esterases, the hydrolytic cleavage of carboxyl esterases, and the occurrence and distribution of phosphohydrolases. A chapter discussing the two groups of lipolytic enzymes (the first containing enzymes of broad substrate specificity and not requiring cofactors; the second containing metalloenzymes with very narrow substrate requirements) concludes this book.
This book is a valuable resource for chemists, biochemists, and those working in the field of nutritional sciences.