title: Modification of polysaccharides and plant cell wall by endo-1,4-beta-glucanase and cellulose-binding domains.
abstract: Cellulose is one of the most abundant polymers in nature. Different living systems evolved simultaneously, using structurally similar proteins to synthesize and metabolize polysaccharides. In the growing plant, cell wall loosening, together with cellulose biosynthesis, enables turgor-driven cell expansion. It has been postulated that endo-1,4-beta-glucanases (EGases) play a central role in these complex activities. Similarly, microorganisms use a consortium of lytic enzymes to convert cellulose into soluble sugars. Most, if not all, cellulases have a modular structure with two or more separate independent functional domains. Binding to cellulose is mediated by a cellulose-binding domain (CBD), whereas the catalytic domain mediates hydrolysis. Today, EGases and CBDs are known to exist in a wide range of species and it is evident that both possess immense potential in modifying polysaccharide materials in-vivo and in-vitro. The hydrolytic function is utilized for polysaccharide degradation in microbial systems and cell wall biogenesis in plants. The CBDs exerts activity that can be utilized for effective degradation of crystalline cellulose, plant cell wall relaxation, expansion and cell wall biosynthesis. Applications range from modulating the architecture of individual cells to an entire organism. These genes, when expressed under specific promoters and appropriate trafficking signals can be used to alter the nutritional value and texture of agricultural crop and their final products. EGases and CBDs may also find applications in the modification of physical and chemical properties of composite materials to create new materials possessing improved properties.
authors.affiliation: The Faculty of Agricultural, Food and Environmental Quality Sciences, The Institute of Plant Science and Genetics in Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel.
authors.forename: Ilan
authors.initials: I
authors.lastname: Levy
authors.forename: Ziv
authors.initials: Z
authors.lastname: Shani
authors.forename: Oded
authors.initials: O
authors.lastname: Shoseyov
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002473:Cell Wall / Q000378:metabolism; D002482:Cellulose / Q000378:metabolism*; D006026:Glycoside Hydrolases; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism; D059828:Plant Cells; D010940:Plant Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D011134:Polysaccharides / Q000378:metabolism*; D021122:Protein Subunits; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000145:classification* / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D010940:Plant Proteins; D011134:Polysaccharides; D021122:Protein Subunits; D002482:Cellulose; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase; C094192:arabinogalactan endo-1,4-beta-galactosidase