Review: The structure and function of cellulase (endo-β-1,4-glucanase) and hemicellulase (β-1,3-glucanase and endo-β-1,4-mannase) enzymes in invertebrates that consume materials ranging from microbes, algae to leaf litter

Publication date: February 2020Source: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Volume 240Author(s): Stuart M. LintonAbstractThis review discusses the reaction catalysed, and the structure and function of the cellulase, endo-β-1,4-glucanase and the hemicellulase enzymes, β-1,3-glucanase and endo-β-1,4-mannase that are present in numerous invertebrate groups with a diverse range of feeding specialisations. These range from microbial deposit and filter feeders, micro and macrophagous algal feeders, omnivores to herbivorous leaf litter and wood feeders. Endo-β-1,4-glucanase from glycosyl hydrolase family 9 (GH9) digests cellulose like β-1,4-glucans from a range of materials. As it hydrolyses crystalline cellulose very slowly, it is a poor cellulase. Where tested, the enzyme has dual endo-β-1,4-glucanase and lichenase activity. Its presence does not necessarily indicate the ability of an animal to digest cellulose. It only indicates the ability to digest β-1,4-glucans and its function, which is discussed in this review, should be considered with reference to the substrates present in the diet. β-1,3-glucanase (laminarinase) belongs to glycosyl hydrolase family 16 (GH16) and hydrolyses β-1.3-glucans. These polysaccharides are present in the cell walls of algae, protozoans and yeast, and they also occur as storage polysaccharides within protozoans and algae. Depending on their site of expression, these enzymes may function as a di...
Source: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Category: Molecular Biology Source Type: research