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Abstract
Pectins are one of the classes of complex structural plant cell wall polysaccharides. They are localized in the middle lamella and primary cell wall of higher plants. Pectins have a long-standing use as gelling agents whereas their enzymatic degradation or modification plays an important role in the processing of agricultural crops and the manufacturing of foods and beverages. Progress in pectin and pectinase research has been most prominent in two areas over the past 5 years. The first one concerns the analysis and elucidation of the complex chemical structure of pectin and identification of novel enzymes involved in the degradation of these structures. The second area concerns the mode of action and the 3-dimensional structure of various pectin degrading enzymes as well as the cloning of a large number of genes encoding enzymes involved in pectin degradation and modification. This book covers the following topics. First the structural, physical and chemical properties of pectin are treated followed by information about its biosynthesis and about the biological effects of pectin and its degradation products in biological systems such as plant-pathogen interactions and human nutrition. Identification of novel enzymes, the mode of action of different pectinases and the 3-D structure of bacterial pectate lyases forms the second block. This is followed by the genetics and regulation of pectinase biosynthesis in saprophytic and phytopathogenic microbial systems as well as in plant systems. Finally, developments in pectin manufacturing and application of pectinases in traditional (food, beverage) and novel technologies are treated. This book is meant for those actively involved in fundamental and applied aspects of pectin and pectinase research but it is also of value for those interested in plant cell wall biosynthesis and architecture, phytopathology, food technology and human nutrition. This book not only reflects the present status of research in the field but it will turn out to be a very useful reference work as well.